ID A0A0G1N6D2_9BACT Unreviewed; 459 AA.
AC A0A0G1N6D2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KKT88607.1};
GN ORFNames=UW89_C0006G0015 {ECO:0000313|EMBL:KKT88607.1};
OS Parcubacteria group bacterium GW2011_GWB1_45_10.
OC Bacteria.
OX NCBI_TaxID=1618877 {ECO:0000313|EMBL:KKT88607.1, ECO:0000313|Proteomes:UP000033817};
RN [1] {ECO:0000313|EMBL:KKT88607.1, ECO:0000313|Proteomes:UP000033817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT88607.1}.
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DR EMBL; LCKC01000006; KKT88607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1N6D2; -.
DR STRING; 1618877.UW89_C0006G0015; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR Pfam; PF03734; YkuD; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KKT88607.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:KKT88607.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..198
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT DOMAIN 211..440
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 246
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 459 AA; 51778 MW; E45B34673ADA58DD CRC64;
MLKKFLQKQI PFSAAFLVIL MVSALSAGLF FVFRNKIYQY QLYLVDSEKP SSIFNLEYGS
LPKMSEESFF LRIKNQLISD KASFIEANLS EMELKFFDRG QETKKFKIIG KGLDGSWWET
PAGIYKIETK EKVHFSSIGQ VYMPYSMQFQ GNFFIHGVPY YPDGRETNLN YTGGCIKLLT
KDAREIFELS SLGIPVLVFE KDFQKDGFVH EVQAPKVSAQ SYLAADLKNN FVFFEKNSSS
VLPIASLTKL MTAVIATEYV NLEKEIEVTQ AMLAPTSVPR LKIGQTYKAY DLLFPLMTES
SNEAAQALSY FLGPQMFVEL MNKKAESLDM ESTVFADSSG ISPVSAASAK NLFSLAKYLY
FNRQFVLSLT NNSIDTSVYG APKFSYLSNF NKPGNSSSIW KQFVGGKIGL TKASEQTIVS
VFELELKNEK RPVAIIVLGS NNNFKDVEEI ISRIKTFYE
//
