ID V5FH66_9VIBR Unreviewed; 393 AA.
AC V5FH66;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN Name=dacA {ECO:0000313|EMBL:GAD91083.1};
GN ORFNames=VHA01S_067_00180 {ECO:0000313|EMBL:GAD91083.1};
OS Vibrio halioticoli NBRC 102217.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219072 {ECO:0000313|EMBL:GAD91083.1, ECO:0000313|Proteomes:UP000017800};
RN [1] {ECO:0000313|EMBL:GAD91083.1, ECO:0000313|Proteomes:UP000017800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD91083.1,
RC ECO:0000313|Proteomes:UP000017800};
RA Ichikawa N., Kimura A., Ohji S., Hosoyama A., Fujita N.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAD91083.1, ECO:0000313|Proteomes:UP000017800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD91083.1,
RC ECO:0000313|Proteomes:UP000017800};
RA Isaki S., Kimura A., Ohji S., Hosoyama A., Fujita N., Hashimoto M.,
RA Hosoyama Y., Yamazoe A.;
RT "Whole genome shotgun sequence of Vibrio halioticoli NBRC 102217.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:GAD91083.1}.
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DR EMBL; BAUJ01000067; GAD91083.1; -; Genomic_DNA.
DR RefSeq; WP_023405383.1; NZ_BAUJ01000067.1.
DR AlphaFoldDB; V5FH66; -.
DR eggNOG; COG1686; Bacteria.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000017800; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:GAD91083.1}; 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:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..393
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004732869"
FT DOMAIN 284..374
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 68
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 393 AA; 42956 MW; 5422DAD88FAE8339 CRC64;
MKKITQSLKS LAVTSALASI AFSAVSQAAP IVLPDAPQIA AKGYVLMDFN SGKVIAQKEA
NTKLHPASLT KMMTSYVIGQ ELKRGNISKD DEVVVSKNAW AKNFPDSSKM FIEVGTTVTV
DKLNHGIIIQ SGNDACVAMA EHVAGSEDAF VDLMNAWAKS IGMKNSHFAN VHGLDNDGLF
STPYDMALLG QALIRDVPDE YAIYSQKQFT YNGITQYNRN GLLWDKSMHV DGIKTGHTSG
AGYNLVSSGT EGQMRLVAVV MGTKSSNARK AESKKLLNYG FRFFETVAPH KKGEVFAEEK
IWMGSQDTVK LGLAEDTYVT LPRGVAKNLK ASFVLDKELK APIKKGDVVG RVFYQVDGQD
IAQYPLLSLE DVNEGGLFSR LIDYLVLLFN SWF
//
