MyMpn
The Mycoplasma pneumoniae database
 
e.g Mpn001 or dnaN or polymerase
Gene pmsR (MPN607)
Name 
pmsR
Stable ID 
MPN607
Location 
727599 - 728072 +
Sequence 
    1  ATGAAACAAA TCTATTTTGG TGGTGGCTGT TTTTGGGGTA CCCAAAAGTA TTTTGATCTG
   61  ATTAAGGGTG TCCAAAAGAC CAGTGTGGGC TACCTCAATT CCAACATGAA AAATCCCACT
  121  TACGAACAAG TATGTAGTGG GCAGACCAAC GCAGTGGAAG CAGTGTTCGT TGAATATGAT
  181  GAAAACAAGG TAAGCTTAAA CGAACTTATT GATGCTTTCT TTAAGGTCAT TGATCCCACC
  241  ATTAGAAACC GTCAGGGTAA TGATATTGGT ACCCAGTACC GTACCGGAGT TTATTGGGTA
  301  GATCCCCAAG ACGAGCAGTT AATTACGCAA AAGTTTAGGG AACTACAGGC CAATTATCCA
  361  AAACCAATTG TGACGGAAAA CCGTGCAATG GAAAACTATT TTTTAGCAGA AGAGTACCAC
  421  CAGGATTACT TAAAGAAAAA TCCTCATGGT TACTGTCACA TTAAATTTGA CTAG
Download Sequence
Operon 
OP245
Operon location 
727575 - 728050
Protein (mpn607)
Name 
Peptide methionine sulfoxide reductase msrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase)
Stable ID 
Mpn607
Molecular Weight 
17270
Isoelectric Point 
6
Localization 
Cytoplasm
Comment PHOSPHORYLATED
Sequence 
MKQIYFGGGCFWGTQKYFDLIKGVQKTSVGYLNSNMKNPTYEQVCSGQTNAVEAVFVEYDENKVSLNELIDAFFKVIDPT
IRNRQGNDIGTQYRTGVYWVDPQDEQLITQKFRELQANYPKPIVTENRAMENYFLAEEYHQDYLKKNPHGYCHIKFD
Post translational modifications
Modification Modified sequence Relative start Relative end Amino acid
Oxidation AmENYFLAEEYHQDYLK 129 146 M
GENE/PROTEIN pmsR (Domains Overview)
Click on the features to jump to domain info

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Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
1-152 PTHR10173 (n.a.) NULL 9.3887e-44
1-153 G3DSA:3.30.1060.10 (IPR002569) Peptide methionine sulphoxide reductase MsrA Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0019538'>'protein' == '' ? '': 'protein'; 'metabolic' == '' ? '': 'metabolic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0019538) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:'oxidoreductase' == '' ? '': 'oxidoreductase';'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity';

0
1-154 SSF55068 (IPR002569) Peptide methionine sulphoxide reductase MsrA Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0019538'>'protein' == '' ? '': 'protein'; 'metabolic' == '' ? '': 'metabolic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0019538) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:'oxidoreductase' == '' ? '': 'oxidoreductase';'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity';

0
2-152 TIGR00401 (IPR002569) Peptide methionine sulphoxide reductase MsrA Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0019538'>'protein' == '' ? '': 'protein'; 'metabolic' == '' ? '': 'metabolic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0019538) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:'oxidoreductase' == '' ? '': 'oxidoreductase';'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity';

0
2-155 PF01625 (IPR002569) Peptide methionine sulphoxide reductase MsrA Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0019538'>'protein' == '' ? '': 'protein'; 'metabolic' == '' ? '': 'metabolic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0019538) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:'oxidoreductase' == '' ? '': 'oxidoreductase';'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity';

0
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
2 157 155 - MAG3130 Mycoplasma agalactiae 3 155 7e-35 46.1538 345
1 156 155 - MARTH_orf807 Mycoplasma arthritidis 1 156 <1e-50 53.2051 448
9 154 145 - Caulobacter crescentus NA1000 53 202 9e-29 41.3333 298
6 147 141 - Caulobacter crescentus NA1000 32 173 1e-19 36.8056 219
1 157 156 - MCJ_001120 Mycoplasma conjunctivae 1 156 1e-36 45.8599 361
6 151 145 - Lactococcus lactis subsp. lactis KF147 8 155 2e-22 34.8993 242
6 153 147 - Lactococcus lactis subsp. lactis KF147 8 157 1e-23 35.3333 252
6 151 145 - Bacillus subtilis subsp. subtilis 10 157 1e-22 35.8108 247
6 151 145 - Bacillus subtilis subsp. subtilis 10 157 8e-23 35.8108 249
2 153 151 - Rv0137c Mycobacterium tuberculosis 5 155 1e-24 35.4839 263
1 148 147 - b4219 Escherichia coli 43 195 2e-26 37.9085 278
1 157 156 - MG408 Mycoplasma genitalium 1 157 <1e-50 77.0701 681
2 157 155 - MCAP_0722 Mycoplasma capricolum subsp. capricolum 3 155 1e-35 45.5128 352
1 154 153 - MMOB4950 Mycoplasma mobile 9 161 2e-32 43.5065 324
2 157 155 - MSC_0774 Mycoplasma mycoides subsp. mycoides SC 3 155 2e-35 45.5128 351
6 151 145 - LIC_12978 Leptospira interrogans serovar Copenhage 30 177 2e-22 35.1351 244
1 153 152 - LIC_10545 Leptospira interrogans serovar Copenhage 13 166 2e-31 36.3636 321
1 157 156 - MYCGA7010 Mycoplasma gallisepticum 2 160 <1e-50 53.4591 457
1 156 155 - MYPE5610 Mycoplasma penetrans 2 157 <1e-50 57.0513 487
2 157 155 - Mycoplasma pulmonis 3 157 1e-31 41.25 319
External IDs
EC number 
1.8.4.11
Gene ID 
876738
GI 
13508346
GO 
Post-translational modification, protein turnover, chaperones/ Defense mechanisms
Home COG 
OV
InterPro 
IPR002569|Methionine sulfoxide reductase A
Old MP number 
MP235
Pathway 
Regulation
Pathway 
Oxygen radical stress
PDB homologs 
1fva_A
PDB homologs 
1fvg_A
PDB homologs 
1ff3_A
Pfam 
PF01625
PID 
g1673902
RefSeq 
NP_110296.1
Swiss-Prot protein ID 
MSRA_MYCPN
phylomeDB tree 
MSRA_MYCPN
UniProt 
P75188
Transcription
IMAGE BROWSERS

OPERON OP245 (Genomic Overview)
Region:727575-728050

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STRING image

STRING of Mpn607STRING legend

PDB image(s)

1fva

PDB 1fva

1fvg

PDB 1fvg

1ff3

PDB 1ff3
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