ID D8F3A2_9DELT Unreviewed; 418 AA.
AC D8F3A2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EFK09748.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:EFK09748.1};
GN Name=dacB {ECO:0000313|EMBL:EFK09748.1};
GN ORFNames=NPH_3938 {ECO:0000313|EMBL:EFK09748.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK09748.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK09748.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK09748.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:EFK09748.1}.
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DR EMBL; ADZZ01000271; EFK09748.1; -; Genomic_DNA.
DR AlphaFoldDB; D8F3A2; -.
DR Proteomes; UP000003834; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EFK09748.1};
KW Hydrolase {ECO:0000313|EMBL:EFK09748.1};
KW Protease {ECO:0000313|EMBL:EFK09748.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003834}.
SQ SEQUENCE 418 AA; 46663 MW; CA21010B89CA82F9 CRC64;
MANPIPIKKR VLKKWVSLSC AFFLCQILIL FYPHGAKAKK WLPCNQQIKT TDSFLLATPQ
GKVLFEKNAD KQRVPASTLK ILTSLAALDH FGTSYRFTTE FYKDKSGNLK IKGYGDPLLV
SEALTQIAEI LAGNGEPFRN IILDDTYFER EIHVPGCDNT TNPYDAPIGA LCANFNTVAF
RTGKNGGFYS TERQTPMIPF MIRQIRSQGL RSGRRTFTHD SKVAALYVGE LLRCLLKKRG
AQVTGKIQFG SVSRKDTLIF TYQSLFPMKT VVRKMLHASS NFMANQIFVA LGAAVYGPPG
TLDKGVRATR AYIKRELGLT HYKIVEGSGL SRKNHLSAYD MLAILEKFKP YKDLLKSQND
VRYKTGSLRG IRTRAGYIES QLGPCCFAVF STGKGQTCPP WSAASKMLWK RLLPPGRG
//
