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
//