ID B0TWI4_FRAP2 Unreviewed; 501 AA.
AC B0TWI4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN OrderedLocusNames=Fphi_0869 {ECO:0000313|EMBL:ABZ87092.1};
OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS O#319-036).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=484022 {ECO:0000313|EMBL:ABZ87092.1};
RN [1] {ECO:0000313|EMBL:ABZ87092.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 25017 {ECO:0000313|EMBL:ABZ87092.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Richardson P.;
RT "Complete sequence of chromosome of Francisella philomiragia subsp.
RT philomiragia ATCC 25017.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000937; ABZ87092.1; -; Genomic_DNA.
DR AlphaFoldDB; B0TWI4; -.
DR KEGG; fph:Fphi_0869; -.
DR eggNOG; COG2317; Bacteria.
DR HOGENOM; CLU_032916_1_1_6; -.
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:ABZ87092.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:ABZ87092.1};
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 266
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 501 AA; 58517 MW; 28FED35164632B0C CRC64;
MSEIKSQLQV LKDNLSQKKK YNHVISLMHW DLETEAPKNS INTTSEVIGF FSEKIYEITN
SEEITKSLKY LNNNLSALDE TNKRIVYLTT KQKDRLSKIP KDEYVAYNKL LSQAQNIWTK
ARKDNDFEVF APYLEEIIKY QKKYVERIGY NEHPYDVLLD DYEEGMTVAK LEPFFDSLKE
RIVPLLEKIK DAKQVNTSCI DKPYDIDKQK EYSHKIAKQL GFNFDSGILK ESAHPFTLNF
NKYDVRMTTR YIEDLFTSSL FGTIHETGHA MYEQNIGDNI YDTILGTGVS LGIHESQSRF
YENLVGKNKA FWDCNFSELK SLFAENLTSA NEEDFYKAIN KVSPSLIRVE ADELTYSLHI
LVRFEIEKEI FEKNLDVSEL PKLWNDKYQK YLGIIPNNFS DGILQDVHWS AGLFGYFPTY
ALGSAYASQI FYYMNKEFDV NAAIRENKLE LILSFLTKHI HQFGSLKPAD EIIHDMCGEY
LNAKYYIDYL DDKFSKIYNL K
//
