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Database: UniProt
Entry: A0A1I6SCK3_9SPHI
LinkDB: A0A1I6SCK3_9SPHI
Original site: A0A1I6SCK3_9SPHI 
ID   A0A1I6SCK3_9SPHI        Unreviewed;       903 AA.
AC   A0A1I6SCK3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:SFS74669.1};
GN   ORFNames=SAMN05660206_104221 {ECO:0000313|EMBL:SFS74669.1};
OS   Sphingobacterium wenxiniae.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=683125 {ECO:0000313|EMBL:SFS74669.1, ECO:0000313|Proteomes:UP000198785};
RN   [1] {ECO:0000313|EMBL:SFS74669.1, ECO:0000313|Proteomes:UP000198785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22789 {ECO:0000313|EMBL:SFS74669.1,
RC   ECO:0000313|Proteomes:UP000198785};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOZZ01000004; SFS74669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6SCK3; -.
DR   STRING; 683125.SAMN05660206_104221; -.
DR   OrthoDB; 9758209at2; -.
DR   Proteomes; UP000198785; Unassembled WGS sequence.
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; cd06240; 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:SFS74669.1};
KW   Hydrolase {ECO:0000313|EMBL:SFS74669.1};
KW   Protease {ECO:0000313|EMBL:SFS74669.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198785};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..903
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011465259"
FT   DOMAIN          43..333
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   903 AA;  102627 MW;  3ECED1C03A0E6C08 CRC64;
     MKLKIVKHLL IALFISQLSI GQAQHIVSPK EHFGFHIGDD YMLANYKQME SYFKKVAEQS
     DRLIMQDAGV TEEGRQQYLL IISSPENLKN IEKYRSISQR LGRAENLTDE EAKVLAKEGK
     PVVWIDGGMH SNETVGSHQL IETFYQLNNS DDEEILNFLD KVIVLMWHVN PDGQDLLADW
     YMQYQDKEQR NMSIPRLYQK YVGHDNNRDF FMFNMVEATN MAKILYVDWL PQIMYNHHQT
     SPDGTIVAGP PYRDPFNHIF DPLLVTGIDG VGFAMINRLN KEGKPGYVRM DQSTFSTWWN
     GGARTAPYFR NMVGILTETF GSPTPMEVPV VTERLIPKNG LPNPIAPQKW HFKQSIDYSV
     SMNYAILDYA ARNGDELLYN FYQMGKNSIE KGNKDTWTMY PKFAEQLEKT YDEAVKSGQE
     EKKEATGYYR SKIIPTKYYD AVYKNPDNRD PRAYIISADQ ADFATAIKFV NTLIKGGIYV
     YQSKEDFSYG GKHYPKNTIV VKTNQAFRPQ IIDMFEPQDH PHDVQYPGGP PVRPYDAAGW
     TLAMQMGVSY DRIFEDLNIP LERTDYGILL HAPTNSVEVS KVGYAINGKA NDTFIAVNRL
     LKKGVKVSRD EETQNFYVDA KGKAVLDEMA AKYGLTVTSL TQKPSTLTPI NSLKIGLFDH
     YGGSMPSGWV RWILEQYEYD YELFYPQDVD SKNIAKYDVL LFIGPGIPVG DKPGITRWGK
     ELEKELVPKE YQPWMGSITK ETSVPILEEY VKNGGRIVTV GSSSGWVYDL GINVTNPLME
     ENKDGKLAEI SSAKYFVPTS ILSAEIDTEK AENYGMAKEA KIVFNNSPVF QFQSTDKLYS
     LGKFTTDKPL LSGWAHGQEY LKDTHLGVVA LLGKGKVVAI GPEITNRAQS HGTFKMLFNQ
     LYK
//
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