ID A0A0S1Y6V6_9BORD Unreviewed; 432 AA.
AC A0A0S1Y6V6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=ASB57_24920 {ECO:0000313|EMBL:ALM85764.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM85764.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM85764.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM85764.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013111; ALM85764.1; -; Genomic_DNA.
DR RefSeq; WP_057654613.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y6V6; -.
DR STRING; 1746199.ASB57_24920; -.
DR OrthoDB; 9778250at2; -.
DR Proteomes; UP000064621; 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; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
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; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 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:UP000064621}.
FT DOMAIN 106..189
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 219..374
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 432 AA; 45474 MW; 2C7F9E20B31BF2F5 CRC64;
MEAWLSTAGA DAALMDDFNA ICAFGGRLSG TGQDTAAIAW ALERMRATGG TVRKVQVPYD
GWRAGRAELQ LLGAEPRTLA CRALLRSAST PDEGLVGEVL DLGQGRVEDF ERAGEAVRGK
IVLVRHEYPF STTHLHRRRK YDQAVARGAI GFLIANPLPG RGVLSGSSGR PRGAAGIPAA
YIDFEGSQAL AAAAAAGQCQ VRLVLTGEEL ENALADLAIL DIPGGTDSRV VISAHMDGHD
LGTSALDNAT GVAVALAAAR ALAPRISART HGLRVCFFTA EEWALTGSAR YLDDMDPAER
ATMKLNVNLD TVAGHSELTA MISEYPALAP FVTAAAADAD TTVDTYLPFM SNSDHANFAR
HGIPALRLTA GFNRPDSNVN NILAAGDVPA VVDEADLRNA LRATCAMAWR GLSMSQEALN
ALTVDSKWTA AK
//
