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
//