ID G0ETJ9_CUPNN Unreviewed; 459 AA.
AC G0ETJ9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Thermostable carboxypeptidase CspA {ECO:0000313|EMBL:AEI76825.1};
DE EC=3.4.17.- {ECO:0000313|EMBL:AEI76825.1};
GN Name=cpsA {ECO:0000313|EMBL:AEI76825.1};
GN OrderedLocusNames=CNE_1c14790 {ECO:0000313|EMBL:AEI76825.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI76825.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI76825.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
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DR EMBL; CP002877; AEI76825.1; -; Genomic_DNA.
DR RefSeq; WP_013956464.1; NC_015726.1.
DR AlphaFoldDB; G0ETJ9; -.
DR KEGG; cnc:CNE_1c14790; -.
DR HOGENOM; CLU_023257_0_1_4; -.
DR Proteomes; UP000006798; Chromosome 1.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:AEI76825.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEI76825.1};
KW Protease {ECO:0000313|EMBL:AEI76825.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..459
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003398468"
FT DOMAIN 249..340
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 459 AA; 49440 MW; A1AD923AEE7DEBCF CRC64;
MAVRDSASRP TTRFALAGLA LAAGLLCNTA QAQTTPAPIS ADTLHAQIET RAKAVEKQLI
AWRRDIHQHP ELGNYETRTA KLVADHLRKL GMEVKTGVAK TGVVGVLKGG KPGPVVALRA
DMDALPVKER VDVPFASKAK GQYLGKEVDV MHACGHDTHV AILMATAEVL AGMKDQLPGT
VKFIFQPAEE SPADFEPNGS NTWGAKQMVS EGVLDNPKVD AIFGLHVSSG IESGKLGWRS
GPSMAAADQF WIDVKGRQTH GARPWGGIDP IVVASQIVMG LQTIQSRQVN AMLEPSVITV
GTIHGGNRMN IVPEKVEMMG TVRTYDEGMK KDIHARMKRT TEAIATSAGA EANFRVVELY
NATINQPALT EKMAPTLQRV AGEGNWMITP KATASEDFSF YQEKVPGLFF NLGVTPKGQD
VTKAPSNHSP EFYVDEPALI NGVRALSSLT VDYMVMAQR
//
