ID D9QBS6_CORP2 Unreviewed; 692 AA.
AC D9QBS6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=M3 family peptidase {ECO:0000313|EMBL:ADL11002.1};
GN ORFNames=CPC231_07755 {ECO:0000313|EMBL:ADL11002.1};
OS Corynebacterium pseudotuberculosis (strain C231).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL11002.1, ECO:0000313|Proteomes:UP000000276};
RN [1] {ECO:0000313|EMBL:ADL11002.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL11002.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21037006; DOI=.1128/JB.01211-10;
RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT strain isolated from a cow in Israel with bovine mastitis.";
RL J. Bacteriol. 193:323-324(2011).
RN [2] {ECO:0000313|EMBL:ADL11002.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL11002.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT "Evidence for reductive genome evolution and lateral acquisition of
RT virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL PLoS ONE 6:E18551-E18551(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001829; ADL11002.1; -; Genomic_DNA.
DR RefSeq; WP_013242398.1; NC_017301.2.
DR AlphaFoldDB; D9QBS6; -.
DR STRING; 681645.CpC231_1537; -.
DR GeneID; 69459678; -.
DR KEGG; cpq:CPC231_07755; -.
DR PATRIC; fig|681645.3.peg.1613; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_11; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000000276; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 3.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000000276};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 232..686
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 692 AA; 75793 MW; 9E6B87946846D68A CRC64;
MTLPVSNPLL EESSLPYQLP PFRDISVEHF LPAFEAALAT HVQEITQITD NAETPSWENT
VEALERSGRD LERVASVFFN LHSTDSSAEM DEIAARVAPL LAEHSDAIYL NSELFTRLEA
VAAPEDAESK RLHEHVLRTF RRHGAGLGES EMARLREINS RLSVLADSFG RNLLADTKAL
AAQFPHGEEL EGLSPGRLAS AAADAEAAGV DGFVIPLELP TVQAEQGSLV RHEARARLYE
ASQRRGAESN AEIVVETVQL RAERAALLGY QTHADYVIAE ETAGSAAAAR DLLFDLAPAA
AANARGEYKL LDEASRGESE EWAQESTMEG ADWPYWESKV RARDFALDEE KLSQYFPLQQ
VLRDGVFYAA NRLYGITVIS RPDLDGYAEG VEVWEVKDAN GEGIGLFLTD YFGRSSKRGG
AWMSSFMNQS DLLGTKPVVV NVMGITKPAD GSDALLSIDS LRTVFHEFGH ALHGLLSKVR
YPTFSGTSVP RDYVEFPSQI NENWAFDPAI LKNFARHVDT GEVIPDELVA AIGKARQFGQ
GFATTEYLSA AVIDLAWHSL TQEEAAQLSP SDIAEFERKA LEEAGLDVEH IQPRYKSTYF
NHIFSGGYSA GYYSYLWAEA LDADGFDWFT EQGAAGVAAS ESAARDAGQK FRDLVLSRGG
ADDFTAAFEA LRGRAKDVGP LLRRRGLAGT VQ
//
