ID A0A086YAD9_9RHOB Unreviewed; 485 AA.
AC A0A086YAD9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KFI31239.1, ECO:0000313|EMBL:QBJ23313.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:QBJ23313.1};
GN Name=dacB {ECO:0000313|EMBL:QBJ23313.1};
GN ORFNames=CN97_09410 {ECO:0000313|EMBL:KFI31239.1}, HmaOT1_02960
GN {ECO:0000313|EMBL:QBJ23313.1};
OS Haematobacter massiliensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Haematobacter.
OX NCBI_TaxID=195105 {ECO:0000313|EMBL:KFI31239.1, ECO:0000313|Proteomes:UP000028826};
RN [1] {ECO:0000313|EMBL:KFI31239.1, ECO:0000313|Proteomes:UP000028826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 47968 {ECO:0000313|EMBL:KFI31239.1,
RC ECO:0000313|Proteomes:UP000028826};
RA Wang D., Wang G.;
RT "Genome of Haematobacter massiliensis CCUG 47968.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBJ23313.1, ECO:0000313|Proteomes:UP000291082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT1 {ECO:0000313|EMBL:QBJ23313.1,
RC ECO:0000313|Proteomes:UP000291082};
RA Lee K.;
RT "The first complete genome sequence of Haematobacter massiliensis OT1
RT isolated from human skin.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; JGYG01000002; KFI31239.1; -; Genomic_DNA.
DR EMBL; CP035510; QBJ23313.1; -; Genomic_DNA.
DR RefSeq; WP_035707550.1; NZ_NIPY01000017.1.
DR AlphaFoldDB; A0A086YAD9; -.
DR STRING; 195105.CN97_09410; -.
DR KEGG; hml:HmaOT1_02960; -.
DR eggNOG; COG2027; Bacteria.
DR OrthoDB; 5372081at2; -.
DR Proteomes; UP000028826; Unassembled WGS sequence.
DR Proteomes; UP000291082; Chromosome.
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; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KFI31239.1};
KW Hydrolase {ECO:0000313|EMBL:QBJ23313.1};
KW Protease {ECO:0000313|EMBL:KFI31239.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028826};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..485
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036290749"
SQ SEQUENCE 485 AA; 51173 MW; 69DBEAF23DA3B585 CRC64;
MTRSPSLSRR SLLALLLAAP AGAACARAPE TAVRPPSRPG PADLDALLAR ARLGAEVSFM
LADPATGEVL EARDPTAAVP PASVSKTITT LYAWETLGSA HRFATRLLAT GPIRDGVVQG
DLILAGGGDP MLSSDDLGDM AEALRQQGVR GVTGAFRTWS GALPYVEQID PAQPAHVGYN
PAVSGLDLNF NRVQFFWQRQ GGGITTRMEA TGDRFRPQVR MARMRLADRD TPLFTFSGGN
GTDDWTVAAR ALNAKGSRWL PVRSSAAYAG EAFRTLAAQR GITLGPPVPL AGAVQGTALV
THSSDDLAAI AADMLKFSNN LTAETLGLTA TLARGGKAGS LASSAGEMSA WARARFGAAG
IDLVDHSGLG GESRVTAAAM VRVLSGGGVL PTLLRRYDLP AGFGREPHPV EVRAKTGTLN
FASGLAGYIL TPGRPLVFAM FMADLDRRRA LSRQERENPP GALEWTSRAR RFQQELLARW
IAVST
//
