ID A0A0H4WEI7_9BORD Unreviewed; 483 AA.
AC A0A0H4WEI7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AKQ54806.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:AKQ54806.1};
GN Name=dac {ECO:0000313|EMBL:AKQ54806.1};
GN ORFNames=ACR54_01481 {ECO:0000313|EMBL:AKQ54806.1};
OS Bordetella hinzii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ54806.1, ECO:0000313|Proteomes:UP000036382};
RN [1] {ECO:0000313|EMBL:AKQ54806.1, ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|EMBL:AKQ54806.1,
RC ECO:0000313|Proteomes:UP000036382};
RX PubMed=26316634;
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT Humans.";
RL Genome Announc. 3:e00965-e00915(2015).
RN [2] {ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL Submitted (JUL-2015) 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; CP012076; AKQ54806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4WEI7; -.
DR STRING; 103855.ACR54_01481; -.
DR KEGG; bhz:ACR54_01481; -.
DR PATRIC; fig|103855.14.peg.1420; -.
DR eggNOG; COG2027; Bacteria.
DR Proteomes; UP000036382; 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 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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AKQ54806.1};
KW Hydrolase {ECO:0000313|EMBL:AKQ54806.1};
KW Protease {ECO:0000313|EMBL:AKQ54806.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036382};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005211686"
SQ SEQUENCE 483 AA; 51310 MW; 922F0EC7D35614F7 CRC64;
MGYLAWGRAC LALGMTLAAL LPGVGRAQGP AGALGLPASL AQAWKATKLP DDALSLVVQE
VNGPRLVAIN AKAPRNPASV MKLVTTWAAL SELGPNYVWR TDFLTEPGAR PDAHGVLKAP
LYWRAGGDPQ LLLQDLWTLL RELRLRGVKE ISDLVVDRSI FGQVATDPGA FDGAPDRAYN
ASPDALMVGF GALRLLVTPD AAARKWVATV DPPVPGLRLE GEVQWSEARC PGPPVVATQP
VVTQQGVTLR LSGSVAGSCG EFSLYRLALS QQEYTDAVFR LLWRELGGTF KGKMRAGVVP
ADAVVLASHE SPTLGEAIRV INKRSNNVMA RTLLLTLGAE RGRRPATVAS SESVAKDLLS
RQGLDMPELV IDNGAGLSRE ARVSADSLAS LLTLAWRSPV MPEYLASMAI AGVDGTVRRR
MKGNGALGMA HLKTGSLRDV RSIAGYVLGN SGKRFVVVSI VNHDNAGAVR SFDDALIAWL
AEQ
//
