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Database: UniProt
Entry: A0A1D9MDH9_9RHOB
LinkDB: A0A1D9MDH9_9RHOB
Original site: A0A1D9MDH9_9RHOB 
ID   A0A1D9MDH9_9RHOB        Unreviewed;       475 AA.
AC   A0A1D9MDH9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:AOZ69911.1};
GN   ORFNames=LPB142_11740 {ECO:0000313|EMBL:AOZ69911.1};
OS   Rhodobacter sp. LPB0142.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1850250 {ECO:0000313|EMBL:AOZ69911.1, ECO:0000313|Proteomes:UP000176562};
RN   [1] {ECO:0000313|EMBL:AOZ69911.1, ECO:0000313|Proteomes:UP000176562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0142 {ECO:0000313|EMBL:AOZ69911.1,
RC   ECO:0000313|Proteomes:UP000176562};
RA   Kim E., Yi H.;
RT   "Rhodobacter sp. LPB0142, isolated from sea water.";
RL   Submitted (OCT-2016) 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; CP017781; AOZ69911.1; -; Genomic_DNA.
DR   RefSeq; WP_071166485.1; NZ_CP017781.1.
DR   AlphaFoldDB; A0A1D9MDH9; -.
DR   STRING; 1850250.LPB142_11740; -.
DR   KEGG; rhp:LPB142_11740; -.
DR   Proteomes; UP000176562; Chromosome.
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:AOZ69911.1};
KW   Hydrolase {ECO:0000313|EMBL:AOZ69911.1};
KW   Protease {ECO:0000313|EMBL:AOZ69911.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176562}.
SQ   SEQUENCE   475 AA;  50117 MW;  2885173283285478 CRC64;
     MAIDRRHFLT AASAAALTAV GGGAGWAAGG AEDLVAQAGL SGEVSYLVAD LKSGLVLESR
     NPNLGMPPAS TAKAITSLYA LETLGPEYRF RTRVIATGPV RGGTLEGDLV LAGGGDPTLS
     TDDLGDLAAR LVAKGVRAVR GRLLVWGGAL PYAAQIAGDQ PVYVSYNPSV SGLILNFNRV
     YFEWRRAGSG YQLGMDARGE RFQPRAYSTD VALAQRQSPL FTYSEQGGKE HWTVAAGALG
     RGGSRWLPVR HPELYAGDVF QTLARAQGLD LPAPQPVSSL PRGEILVERG SDPLGRILVD
     MLKYSTNVTA EAVGMTTSVA RGAPAALGRS GASMSGWLTQ RLGGGGARFV DHSGLGAETR
     ISASEMVHAL AALGPRVGLR GLMKGFKLRD DDGKILQNQS LRVDAKTGTL NFVSSLAGYM
     TAPDGTELVF AIFTGDLARR RAAAQVEQPA GGRDWVRRSK ILQSRLIERW AALYG
//
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