ID D4BR21_BIFBR Unreviewed; 466 AA.
AC D4BR21;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EFE88666.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:EFE88666.1};
GN Name=dacB {ECO:0000313|EMBL:EFE88666.1};
GN ORFNames=BIFBRE_04554 {ECO:0000313|EMBL:EFE88666.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE88666.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE88666.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE88666.1,
RC ECO:0000313|Proteomes:UP000003191};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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:EFE88666.1}.
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DR EMBL; ACCG02000012; EFE88666.1; -; Genomic_DNA.
DR AlphaFoldDB; D4BR21; -.
DR STRING; 1685.RY69_314; -.
DR MEROPS; S13.004; -.
DR PATRIC; fig|518634.7.peg.1524; -.
DR HOGENOM; CLU_017692_0_2_11; -.
DR Proteomes; UP000003191; 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; 3.40.710.10; 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:EFE88666.1};
KW Hydrolase {ECO:0000313|EMBL:EFE88666.1};
KW Protease {ECO:0000313|EMBL:EFE88666.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003191}.
FT REGION 231..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 47495 MW; FDE913166CC8983B CRC64;
MLITIALFAG YCIADVYDVM PGMLTLKPVD APTFADPVSA KQGGTIAGSL DATKTIDAAA
AGEVMNELLA AEGVGSDVSV VVEDARGTVA AEHESGTPRE PASTMKTLTA LAASSTLNMA
ATLDTQVFLT QSDTGSDTVT LKGNGDMLLS AGDSDADHIN GRAGLNTLAQ ATAAALAQRG
ITTVHVNYDD TLFGDSRIPT GLRNADGGVL GEYTTYFTSV SSMAIDGGRQ YSDSMPAPAN
PDASAGYPEL SPHTAADVAA TFSGLLQQHG ITVEAEPAAH AAPQGASPIT SVSSATLSEI
LAFMLRHSDN TLAEEFGRLT ALARSENNSP EGATKAVRTV LGNLKIDING LTMADCSGLS
PGSQLTVRTL AAVQQRNLTV GDGAPAAEGL SVAGLVGSAR KRYTSDDVAG LLRVKTGSLD
TVTSMAGNVS RTHGGALSFA VVINNPADYW AASNAISAFI TKLAEL
//
