ID V4NU93_9CAUL Unreviewed; 488 AA.
AC V4NU93;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=ABAC402_03715 {ECO:0000313|EMBL:ESQ76780.1};
OS Asticcacaulis sp. AC402.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282361 {ECO:0000313|EMBL:ESQ76780.1, ECO:0000313|Proteomes:UP000017812};
RN [1] {ECO:0000313|EMBL:ESQ76780.1, ECO:0000313|Proteomes:UP000017812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC402 {ECO:0000313|EMBL:ESQ76780.1,
RC ECO:0000313|Proteomes:UP000017812};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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}.
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:ESQ76780.1}.
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DR EMBL; AWGC01000006; ESQ76780.1; -; Genomic_DNA.
DR RefSeq; WP_023448318.1; NZ_AWGC01000006.1.
DR AlphaFoldDB; V4NU93; -.
DR STRING; 1282361.ABAC402_03715; -.
DR PATRIC; fig|1282361.3.peg.733; -.
DR eggNOG; COG2234; Bacteria.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000017812; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017812};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..488
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004723802"
FT DOMAIN 275..470
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 488 AA; 51661 MW; AA46D2E2455DC964 CRC64;
MKPIHFAAAL AAGLAVAATP VWARPKKATT VAAAPSALAP AEQAASLRDA ALKDNNAYEF
VAELTTRFGA RPAGSASETA AAQWSAEQLK AMGFDNVRIE TFPLEIWQRG DEQLEMVGPF
PQKLIATALG GSGTTPPQGV EAEAVLFETY DRFNTSTIDL KGKIVVILQP TVATQTGVGY
GVNSGSVRRQ GPEIARQRGA VGYIMRSLGT HDHRFPHTGG TRFLGADGVP AMAISPPDAE
QLERVLKLQK DGKAGPIRLK MLSTPKFLGT GQSQNVIAEI TGAKRPQEII TIGGHLDSWD
LGTGAIDDGA GVAITMAAAK TILDSKVRPD RTIRVVFWGS EEVSQPNDRG LTGANAYATA
YRAEFPNHII AAESDFGAGV VYSLSLPATD STDFTKQIGN VLYPLGIFVD KAVSTGGGPD
TTPLFNAGVP VMDLNQDGMD YFDTHHTPDD VLERIDPVKM DQNVAAWAAT VWLIAATDVK
FKGVAPAN
//
