ID Q5HN55_STAEQ Unreviewed; 413 AA.
AC Q5HN55;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Aminopeptidase family protein {ECO:0000313|EMBL:AAW54774.1};
GN OrderedLocusNames=SERP1417 {ECO:0000313|EMBL:AAW54774.1};
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW54774.1, ECO:0000313|Proteomes:UP000000531};
RN [1] {ECO:0000313|EMBL:AAW54774.1, ECO:0000313|Proteomes:UP000000531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531};
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J., Khouri H., Utterback T., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K., Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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DR EMBL; CP000029; AAW54774.1; -; Genomic_DNA.
DR RefSeq; WP_001832467.1; NC_002976.3.
DR AlphaFoldDB; Q5HN55; -.
DR STRING; 176279.SERP1417; -.
DR MEROPS; M29.005; -.
DR GeneID; 50018336; -.
DR KEGG; ser:SERP1417; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_054346_1_0_9; -.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:AAW54774.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000531}.
SQ SEQUENCE 413 AA; 46846 MW; AE5EEBDE3EE1833D CRC64;
MTNYHNKLKQ YAELLVRVGM NVQPQQPVFI RSSVEALELT HLIVEEAYKA GAEDVRVSYT
DPKLKRLKFE NESVEHFEKQ ELKQYDIEER LDYVNRGAAN LALIAEDPEL LNGIDAQKLK
AYQTVYSKGF KPYMEASQKN QFPWVVAAFP TRDWARRVYP ELDVESAYIK FIDEVFDIVR
VDGQNPIENW EKHIKDLSVH AKRLQEKNYQ ALHYISEGTD LIVGLPKGHI WEDATSYVNG
DGQPFIANIP TEEVFTAPDR NNVNGYVTNK LPLNLNGNII DGFTLTFKDG VIIDVKAEKG
EKLLKDLIAT DEGACRLGEV ALVPDDSPIS NRRTIFYNTL FDENASCHLA IGSAYSFNIK
GGTEMTTEEK IANGLNDSNI HEDFMIGSPD LTIYGILQDE TKELVFKNGN WAK
//
