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Database: UniProt
Entry: V6F756_MAGGM
LinkDB: V6F756_MAGGM
Original site: V6F756_MAGGM 
ID   V6F756_MAGGM            Unreviewed;       496 AA.
AC   V6F756;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   Name=ypwA {ECO:0000313|EMBL:CDL00308.1};
GN   OrderedLocusNames=MGMSRv2__3093 {ECO:0000313|EMBL:CDL00308.1};
OS   Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS   / MSR-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=431944 {ECO:0000313|EMBL:CDL00308.1, ECO:0000313|Proteomes:UP000018922};
RN   [1] {ECO:0000313|EMBL:CDL00308.1, ECO:0000313|Proteomes:UP000018922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC   {ECO:0000313|Proteomes:UP000018922};
RX   PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA   Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA   Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA   Wang L., Li J.;
RT   "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL   Genome Announc. 2:e00171-e00114(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}.
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DR   EMBL; HG794546; CDL00308.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6F756; -.
DR   STRING; 1430440.MGMSRv2__3093; -.
DR   KEGG; mgy:MGMSRv2__3093; -.
DR   eggNOG; COG2317; Bacteria.
DR   HOGENOM; CLU_032916_1_1_5; -.
DR   Proteomes; UP000018922; Chromosome I.
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:CDL00308.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:CDL00308.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000018922};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        264
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   496 AA;  54434 MW;  B02E0C47145C8BF4 CRC64;
     MSRAYDLLEA RFKKAAILGD ALSVLHWDMS AMMPEGGAEA RAEQLALLKT LSHETLTAPD
     MADLLAAAKA EALDEWERAN LHEMHRDWVH AAALPADLVD AMAKAESTCE MIWRQARPNA
     DFAAVLPSLR EILNLTIQAG QAKAEALGVG IYDALLDQYE PDGRSADIDA VFADLEAFLP
     DFIGQALEAQ AARPEPQLPA GPFPVENQKQ LGQRIMAVLG FDFHHGRQDV SAHPFCGGYP
     EDVRITTRYN TDDFTTALMG VIHETGHALY DFGLPTGKWR YQPVGRARGM QMHESQSLLM
     EMQACRSRGF AGFAAPLMQQ AFDGTGSAWQ PENLYRLGTR VKRGFIRVDA DECTYPAHVI
     IRYGLEKALI EGRMDLADLP GAWNDGYRRL LGITPPDDRL GCLQDIHWYG GSWGYFPTYT
     LGAMSAAQLF AAGLAADPAI ETGIAQGDFV PLLAWLRTHV HGKGSSLSTR DLLVAATGEP
     LDAGVFKAHL QKRYLD
//
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