ID W4Q0Q2_9BACI Unreviewed; 382 AA.
AC W4Q0Q2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:GAE25661.1};
GN ORFNames=JCM9140_1668 {ECO:0000313|EMBL:GAE25661.1};
OS Halalkalibacter wakoensis JCM 9140.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE25661.1, ECO:0000313|Proteomes:UP000018890};
RN [1] {ECO:0000313|EMBL:GAE25661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE25661.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:GAE25661.1}.
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DR EMBL; BAUT01000012; GAE25661.1; -; Genomic_DNA.
DR RefSeq; WP_034744398.1; NZ_BAZN01000012.1.
DR AlphaFoldDB; W4Q0Q2; -.
DR STRING; 1236970.JCM9140_1668; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000018890; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.30.140.30; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:GAE25661.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:GAE25661.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018890};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..382
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004846540"
FT DOMAIN 27..252
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 61
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 382 AA; 43150 MW; 86FA3123D167B2B1 CRC64;
MRKKLALIFI ALLLMGSGIP LQAKAEQRNF SVSAQAAVLI EQESGRVLYG KNEHEPLRIA
SITKIMTAIL AIESGKMDEM VKVSTNAEGT EGSSIYLRAG EKIPLKDLVY GLMLRSGNDS
AVAIAEHVGG SLDGFIYMMN EKAEQIGMVN TMFQNPHGLD DHEDHFSSAH DMALLTQHAM
DNEMYREIAS TKSYRSDGEQ IRVWQNKNRL LTELYEYSTG GKTGYTKRAK RTLVSTATKD
DEHLIAVTLN APSDWHDHMN LFNWAFDTFD LEVLIEEGLL DNIDDEFYKN HVYTPYSFEY
PLSPSEQESL SSKVTLYQPP SKEERDGYIP PQPVGKVEFF IGNDEIGRVP LLYDPPEVEE
KTGFWTRFLD FFSFTIGVRT SD
//
