ID S9R2L6_9RHOB Unreviewed; 489 AA.
AC S9R2L6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=ruthe_01028 {ECO:0000313|EMBL:EPX86218.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX86218.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX86218.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX86218.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
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:EPX86218.1}.
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DR EMBL; AOLV01000010; EPX86218.1; -; Genomic_DNA.
DR RefSeq; WP_021097126.1; NZ_KE557320.1.
DR AlphaFoldDB; S9R2L6; -.
DR STRING; 1123069.ruthe_01028; -.
DR PATRIC; fig|1123069.3.peg.998; -.
DR HOGENOM; CLU_032916_1_1_5; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000015346; 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:EPX86218.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:EPX86218.1};
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:UP000015346};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 255
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 489 AA; 53393 MW; 8A879EEF3F4CADD8 CRC64;
MTAYAELMAF QRETEALAQV MGRLGWDQET VMPPGAAPQR AEEMAALEAV LHARRTDPRL
GDWLAAAVAE DEVAAGNLRI LQRSYERHCK VPARLAAEIA RVTSRAQGIW AEARAAEDVG
AFLPVLSEVV ALRREEGAAI ADGGDPYDAL LDDHEPGARS ADLAAMFARL RPRLVALRAA
MRAAPPAPVL RGPFAEETQM TLAREVATVF GYDFARGRLD KAVHPFSSGS GLDVRITTRT
NPEDPFNCLY ATIHEVGHAT YEQNVDPAHR LTPVGQGASM GVHESQSRLY ENQLGRSRAF
AGWLYGRMRD LFGDFGIASE EAFYRAVNAV RDGHIRTEAD EVQYNLHIML RFDLEQALMR
GDLAVADLEA AWNDRFLADF GFAVERPSQG MLQDVHWSVG LFGYFPTYAL GNVYAGCLHA
ALRAAVPDLD ACLARGEAGP AVAWLRERVH RHGALRPPRE TVAAAAGREP DEGPLLAYLE
EKFGALAGG
//
