ID Q3BQ07_XANC5 Unreviewed; 472 AA.
AC Q3BQ07;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN OrderedLocusNames=XCV3425 {ECO:0000313|EMBL:CAJ25156.1};
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN [1] {ECO:0000313|EMBL:CAJ25156.1, ECO:0000313|Proteomes:UP000007069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10 {ECO:0000313|EMBL:CAJ25156.1,
RC ECO:0000313|Proteomes:UP000007069};
RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneicker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
CC -!- SUBUNIT: Homodimer. The monomeric form is inactive while the homodimer
CC is active. {ECO:0000256|ARBA:ARBA00025833}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371}.
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DR EMBL; AM039952; CAJ25156.1; -; Genomic_DNA.
DR RefSeq; WP_011348389.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BQ07; -.
DR STRING; 456327.BJD11_05610; -.
DR KEGG; xcv:XCV3425; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_033697_1_0_6; -.
DR Proteomes; UP000007069; Chromosome.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR039866; CPQ.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12053:SF3; CARBOXYPEPTIDASE Q; 1.
DR PANTHER; PTHR12053; PROTEASE FAMILY M28 PLASMA GLUTAMATE CARBOXYPEPTIDASE-RELATED; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..472
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004224454"
FT DOMAIN 255..443
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 472 AA; 48774 MW; 22B99DB687F2C2C5 CRC64;
MRRLAVAISA LLACSSALAA QTSIPDSALR TAAQLREQAL ADNTGFSVVQ SLTTEVGPRI
AGGEADPRAV AWAKAKFASL GFDKVWTEPV TFPKWERRSE HAVVIGAHAQ PLTITALGGS
PGGTVEGEVV RFATLAALQA APAGSLAGKI AFVDYQMVKA RDGKDYGNGG AVRSKGPSEA
IRKGAVGFVM RSAGTDSHRV PHTGITRFDE GLTPVPAAAL SVPDANQLAR LTALGSTRLR
LTLDCGWDGT ATSYNVIGEI TGRSKPKEVV VIGGHLDSWD LGTGAIDDGA GVAITMAAGH
LIGQLKQPPK RSIRVVAFAN EEQGLYGGKA YAAAHGTDAK DMALHQIGAE SDFGAGRIYA
FNTGAAAPED SRAATKQIAE VLAPLGIAYE PGKGGPGPDV GPISAKGGAW GWLAQDGTDY
FDLHHTADDT LDKIDPKALA QNVAAYTVFA YLAAEADGDF GSRAKSVQPP SE
//
