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Database: UniProt
Entry: A4CI64_ROBBH
LinkDB: A4CI64_ROBBH
Original site: A4CI64_ROBBH 
ID   A4CI64_ROBBH            Unreviewed;       614 AA.
AC   A4CI64;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Zn-dependent aminopeptidase, putative {ECO:0000313|EMBL:EAR16622.1};
GN   OrderedLocusNames=RB2501_06970 {ECO:0000313|EMBL:EAR16622.1};
OS   Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR16622.1, ECO:0000313|Proteomes:UP000009049};
RN   [1] {ECO:0000313|EMBL:EAR16622.1, ECO:0000313|Proteomes:UP000009049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC   {ECO:0000313|Proteomes:UP000009049};
RX   PubMed=19767438; DOI=10.1128/JB.01191-09;
RA   Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL   J. Bacteriol. 191:7144-7145(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
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DR   EMBL; CP001712; EAR16622.1; -; Genomic_DNA.
DR   RefSeq; WP_015753379.1; NC_013222.1.
DR   AlphaFoldDB; A4CI64; -.
DR   STRING; 313596.RB2501_06970; -.
DR   KEGG; rbi:RB2501_06970; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_015077_1_0_10; -.
DR   OMA; GGMEYAM; -.
DR   OrthoDB; 9814383at2; -.
DR   Proteomes; UP000009049; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09604; M1_APN_like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR034015; M1_LTA4H.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:EAR16622.1};
KW   Hydrolase {ECO:0000313|EMBL:EAR16622.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW   Protease {ECO:0000313|EMBL:EAR16622.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009049};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..614
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002666180"
FT   DOMAIN          345..494
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        355
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        437
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   614 AA;  69986 MW;  C98B1CF94C8B8E2F CRC64;
     MTRLFFLILL ATATAYGQGN TAYWQQHVDY RMEVDMDVET YRYTGTQKLV YTNNSPDTLN
     RVFYHLYFNA FQPGSEMDMR LQAIEDPDGR MTEDGKSRIA GLSPDEIGYL HATSLTQDGT
     ALSYQEEGTV LVVELAEPLL PGSKTTFDME FEGQVPVQIR RSGRNNREGV ALSMSQWYPK
     LAEYDFEGWH ADPYIAREFH GVWGDFDLKL TIDKDYTVGG TGYLQNPQEI GHGYEKPGTS
     VRTRGKTLTW HFKAPNVHDF MWAADPDYLH DTLRLDNGTL LHFLYKDNPE ILENWKNLQP
     KAAATMEFFN RNIGPYPYDQ YSIIQGGDGG MEYAMSTLIT GERSFGSLVG VTVHEMAHSW
     FQHVLATNES RHEWMDEGFT SFISALCMDA VMERQRENPF AGSYNGYRSL AASGREQPLT
     THADRYDFNG GYGISAYSKG AVFLAQLGYV IGQDKLMETI RRYYREFQFR HPTPNDFIRV
     AEKVSGAELE WYLNDFTRTA NTIDYGVKSV EAVEGGTRVS LERIGLMPMP IDLLVALNDG
     TRKTYYLPLR MMRAEKENPY AGFEREVKAD WPWAQPVYDL VLVIPIDEIQ AIAIDPSGLM
     ADIDLENNIW QPGQ
//
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