ID A0A0E3ZFJ7_9BACT Unreviewed; 861 AA.
AC A0A0E3ZFJ7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:AKD03544.1};
GN ORFNames=PKOR_10885 {ECO:0000313|EMBL:AKD03544.1};
OS Pontibacter korlensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD03544.1, ECO:0000313|Proteomes:UP000033109};
RN [1] {ECO:0000313|EMBL:AKD03544.1, ECO:0000313|Proteomes:UP000033109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X14-1T {ECO:0000313|EMBL:AKD03544.1,
RC ECO:0000313|Proteomes:UP000033109};
RX PubMed=26057562; DOI=10.1038/srep10929;
RA Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT "Unraveling adaptation of Pontibacter korlensis to radiation and
RT infertility in desert through complete genome and comparative
RT transcriptomic analysis.";
RL Sci. Rep. 5:10929-10929(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; CP009621; AKD03544.1; -; Genomic_DNA.
DR RefSeq; WP_046310726.1; NZ_CP009621.1.
DR AlphaFoldDB; A0A0E3ZFJ7; -.
DR STRING; 400092.PKOR_10885; -.
DR KEGG; pko:PKOR_10885; -.
DR PATRIC; fig|400092.3.peg.2377; -.
DR HOGENOM; CLU_323582_0_0_10; -.
DR OrthoDB; 9758209at2; -.
DR Proteomes; UP000033109; Chromosome.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06238; M14-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AKD03544.1};
KW Hydrolase {ECO:0000313|EMBL:AKD03544.1};
KW Protease {ECO:0000313|EMBL:AKD03544.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033109};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..861
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002416964"
FT DOMAIN 57..343
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 861 AA; 96658 MW; BEB5CCF7EF20AACB CRC64;
MKNLRVLAVA AMLGLGPVAV AQQAETPLSY YLPAEVSYNS SIPTPKDILG YNVGEWHASH
DQLAMYMRQM ANLSDRITIT EYARTHENRP LYLLTITSPK NHQNLEQIKQ KHRQLSDPSA
SGKLNIKEMP AVVWMGYSVH GNEPSGSNAS LLAVYHLAAA QGPEIDKLLD ETIILIDPSI
NPDGMNRFAS WVNSHRSKNL ITDPNSAEFD EAWPRGRTNH YWFDLNRDWL PLQHPESKGR
LAKFHEWKPN VLTDHHEMGT NATFFFQPGI PSRNNPLTPE NNFKLTQKIG TFHAKALDKI
GSFYYTEESY DDFYYGKGST YPDVNGSVGI LFEQASSRGH AQESVNGVLT FPFTIRNQFT
TTLSTLEAVQ AMREELLAHQ RDFYKQVQNE SKKASTKAYV FGSELDRARA FHLAEIIKQH
QIEVYRPKES FKINNFTYTP ENAYIIPTDQ PQYRLIEAMF ERRTTFQDSL FYDISAWTFP
LAFDLDHAAL SSRNFKSSQL GQKVEDLKLP EGEVVGGKSD YAYTFEWHGY YAPRALNQLM
DRGINTRVAT DKFTTAEGKK YDYGTILIPV AGQSVNAEAL HQIMQEVAQQ NALKVYAMNT
GFNPLGIKLG SPMVLSLKQP KVMMLIGDGV NSYDAGEAWH LMDDRFGMRP VLIKTNDFNR
SEISKYNVVV MAEGSYSNIS KDKLRNWVLQ GGTVVGMGTA AKWLSDNGIG NITFTKSEPD
TAAQKAYADM ANSEGAQVIG GAIFETKLDL THPLAYGYTD EQLPIFRSNT LFMERSKSPY
ANPVMYTANP LMAGYISKPN LQKVKNTAAV DVSTIGAGKV IAMPDNPNFR AFWYGTNKLF
LNSIFFGQII SGNSARAEEA H
//
