ID A5CWX5_VESOH Unreviewed; 375 AA.
AC A5CWX5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=COSY_0433 {ECO:0000313|EMBL:BAF61552.1};
OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Vesicomyosocius.
OX NCBI_TaxID=412965 {ECO:0000313|EMBL:BAF61552.1, ECO:0000313|Proteomes:UP000000247};
RN [1] {ECO:0000313|EMBL:BAF61552.1, ECO:0000313|Proteomes:UP000000247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA {ECO:0000313|EMBL:BAF61552.1,
RC ECO:0000313|Proteomes:UP000000247};
RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA Kato C., Kitagawa M., Kato I., Maruyama T.;
RT "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT clam, Calyptogena okutanii.";
RL Curr. Biol. 17:881-886(2007).
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}.
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DR EMBL; AP009247; BAF61552.1; -; Genomic_DNA.
DR RefSeq; WP_011929822.1; NC_009465.1.
DR AlphaFoldDB; A5CWX5; -.
DR STRING; 412965.COSY_0433; -.
DR KEGG; vok:COSY_0433; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_1_6; -.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000247; Chromosome.
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:BAF61552.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAF61552.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000247};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..375
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002680545"
FT DOMAIN 275..362
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 63
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 375 AA; 41947 MW; 555A826E7BBA69C3 CRC64;
MQNKLFIKFL TILICSFTLN IQAAIFITPK APEISAVAYS IVDYNSGKVI ASNKQHYKRA
PASLTKLMTA YVIFQLISND RIKLEDEVRI SKKAWKTGGS KSFVEVGKTM KLETLLKGMI
IQSGNDSAVA LAEHIAGDES TFTTYMNKYA RKLGMNNSQF RNASGLPDNN QYTTAADIVL
LATAIIKDFP QFYLWYSEKE FTYHGIKQYN RNKLLWNDHT VDGLKTGFTK KAGYNLVASA
KRLGMRLISV VLGSSSVNDR TSQTQKILDY GFRFFETKTI RNIKKELPIA NSTKNMLKVG
TSKIISFTLA RGQFKFSDQV IQLDTALSAP INKGDVVGKL LIQFKGKTMA SIPLIALEHA
QQASFFSRML ETIGF
//
