ID A0A0U4BLD9_9BACT Unreviewed; 852 AA.
AC A0A0U4BLD9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:ALW87387.1};
GN ORFNames=AUC43_14895 {ECO:0000313|EMBL:ALW87387.1};
OS Hymenobacter sedentarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW87387.1, ECO:0000313|Proteomes:UP000059542};
RN [1] {ECO:0000313|EMBL:ALW87387.1, ECO:0000313|Proteomes:UP000059542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5B {ECO:0000313|EMBL:ALW87387.1,
RC ECO:0000313|Proteomes:UP000059542};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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; CP013909; ALW87387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4BLD9; -.
DR STRING; 1411621.AUC43_14895; -.
DR KEGG; hyg:AUC43_14895; -.
DR Proteomes; UP000059542; 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; cd01653; GATase1; 1.
DR Gene3D; 3.40.50.880; -; 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:ALW87387.1};
KW Hydrolase {ECO:0000313|EMBL:ALW87387.1};
KW Protease {ECO:0000313|EMBL:ALW87387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059542};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..852
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006847153"
FT DOMAIN 42..358
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 852 AA; 95655 MW; FDF6B0C5B15D1926 CRC64;
MRNWSVALLT LLSLPSPAQT ATDTGPLLTP DQFLGYKLGT QFTPHAQILR YVDHVVAHTP
SRMKLVRYGS TYEHRPLEVV EIASADNFGR LEDVRHNNLK LAGLEKGSGQ RQQPAVCWLS
YNVHGNEAVS SEAVMQVLYD LANPQDKQMQ DWLKNTVVIV DPCVNPDGRD RYGNWYNRVR
NQSPNANPDS WEHHEPWPGG RFNHYYFDLN RDWAWQTQQE TKQRIVLYNQ WLPAVHADFH
EMGPNNSYYF SPAAKPYHAD ITPWQRKFQD VLGDYNKVVF DKNNWLYFTR ETYDLFAPTY
GDTWPSFNGA IGMTYEQGGG GPAGVAYSRL DGDTLTLGQR IAHHHAASRA TIQATAERHD
DLLREFESYF ATAKSKPQGQ YKSYVLSAGN DPGQLRSLTQ YLERNQISYG FASKRSKTKG
YNYTTGKTES VQIEPRDVVV SMFQPKSTLV KVLFEPRAQL EDSLTYDITS WALPYAFGVK
AYALPGRLDA SGPSPSQATV RGSAAASTDR PYAYLARWNN LQDVRFLSRL LQQKVKVRYA
EKAFESEGQK YAPGTLVITR TGNEAMGPRF DQVVRAQADS AGTIVTAVKS GFSTTGRDLG
SGTVHFVKQP NVAVVAGPGV DGTAFGEVWH FFEQQLGYPI TVLGTDYLSR VSLQKYDVLI
MPNGTYTDVY NDRTLESLKS WVRDGGKLIA MEGAAKMLSN KKDFLLKAKA VDSVAIRKDE
KANPYKLLRR YGNSEREEAE EVVQGSVYRV QLDNTHPLAF GYGDTYFALI RNPLNYRFLG
KGGWNVGVIK KDSYSSGFIG TKARKELTDT FVVGTQDLGR GEVVYLGDNP LFRAFWQGGK
LLFGNAVFLV GQ
//