ID W7AWW6_9LIST Unreviewed; 503 AA.
AC W7AWW6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=MAQA_05268 {ECO:0000313|EMBL:EUJ19584.1};
OS Listeria aquatica FSL S10-1188.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265818 {ECO:0000313|EMBL:EUJ19584.1, ECO:0000313|Proteomes:UP000019246};
RN [1] {ECO:0000313|EMBL:EUJ19584.1, ECO:0000313|Proteomes:UP000019246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1188 {ECO:0000313|EMBL:EUJ19584.1,
RC ECO:0000313|Proteomes:UP000019246};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity,
CC except for -Pro.; EC=3.4.17.19;
CC Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC -!- SIMILARITY: Belongs to the peptidase M32 family.
CC {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUJ19584.1}.
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DR EMBL; AOCG01000006; EUJ19584.1; -; Genomic_DNA.
DR RefSeq; WP_036071759.1; NZ_AOCG01000006.1.
DR AlphaFoldDB; W7AWW6; -.
DR STRING; 1265818.MAQA_05268; -.
DR PATRIC; fig|1265818.5.peg.1044; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000019246; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd06460; M32_Taq; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000313|EMBL:EUJ19584.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000256|PIRSR:PIRSR006615-1};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 267
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 503 AA; 57288 MW; 9B4C7D4ED4BEA4F5 CRC64;
METVAELERD FLAFLKKKSA LSEALNLVYW DIRTKIPKKG AEGRSEVIGV LAGQIFEMEV
SEEMAAFIAA LAPHKDELDE VTRKSLEESS RVYELNKKIP QEEFQAYSKL VADAENVWAE
ARGEDNFAKF EPYLTEIVAF KRKFVEYWGY KDNKYDTLLD QYEPGMTVEI LDEVFGKLRI
AIMELRDKMA KEGTLPDASG LAVPMSEEKQ RAFSEAILAK MGFDFEAGRL DTTVHPFAIG
LNLGDVRITT RYDEANFKMA VFGIIHEGGH AIYEQNIGRN LIGTPLKEGA SMGIHESQSL
FYEIILGSSF AFWKSNYPDL VKQEPAFGKV PLETFYRALN ISESSLVRIE ADILTYPLHI
MIRYELEKAL INGELEVKDL EAAWNDKYEA YLGIRPEKSS EGVLQDIHWA GGDFGYFPSY
ALGLMYAAQF FDAMQKDLKD VEAIVASEDY SEIQEWLTAH IHQYGKLKKP LEILKDTTGE
GLNPDYLITL LNKRYEFVYK LKN
//
