ID A0A0B3S469_9RHOB Unreviewed; 504 AA.
AC A0A0B3S469;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:KHQ55052.1};
GN ORFNames=OA50_00086 {ECO:0000313|EMBL:KHQ55052.1};
OS Mameliella alba.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mameliella.
OX NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ55052.1, ECO:0000313|Proteomes:UP000030960};
RN [1] {ECO:0000313|EMBL:KHQ55052.1, ECO:0000313|Proteomes:UP000030960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ55052.1,
RC ECO:0000313|Proteomes:UP000030960};
RA Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL Submitted (OCT-2014) 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:KHQ55052.1}.
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DR EMBL; JSUQ01000001; KHQ55052.1; -; Genomic_DNA.
DR RefSeq; WP_043135987.1; NZ_JSUQ01000001.1.
DR AlphaFoldDB; A0A0B3S469; -.
DR STRING; 561184.SAMN05216376_10390; -.
DR PATRIC; fig|1515334.3.peg.85; -.
DR OrthoDB; 5372081at2; -.
DR Proteomes; UP000030960; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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 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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KHQ55052.1};
KW Hydrolase {ECO:0000313|EMBL:KHQ55052.1};
KW Protease {ECO:0000313|EMBL:KHQ55052.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030960}.
SQ SEQUENCE 504 AA; 53116 MW; 31FA215F19A35877 CRC64;
MTHGISRRAF LGGVAGAALG GAASPGWARA PETSLRPVAR SDDFRKRIQP PAEALIERAA
LDGEVGFAVA RLHSGEVLET HSPDVSLPPA SVAKALTAGY ALDVLGPAHH FVTRVIATGP
VKDGVVQGDL VLAGGGDPTL DTDALAGLAA AVSAAGVTGL TGGLKVWGGA LPSLIGIDAS
QPDHVGYNPS VSGLNLNYNR VHFEWRKAGS DYTVTMQARS AAHRPDVRVA RMDLIDRSLP
VYTYEDKLGR DNWTVARGAL GDGGARWLPI KKPEAYAGEV FQTLLAAQGI KTGKPEIAAG
LPGGDELARH ESPPLRVILR DMLKWSTNLT AEVVGLAASV ARSGAVPASL QASAAEMNAW
AQEKLGVGGL ALVDHSGLGD QSRVSAMQMM GCLRGLRMKM GIKPLLKDMP LRDSRYQVIE
NAPLKVRAKT GTLNFVSGLA GFVDLPDGTE LVFAIFAADM PRRDALTKAQ RERPEGGRSW
NSRAKILQQG LIGRWGVLYE SDPV
//