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Database: UniProt
Entry: A0A0G1W0H2_9BACT
LinkDB: A0A0G1W0H2_9BACT
Original site: A0A0G1W0H2_9BACT 
ID   A0A0G1W0H2_9BACT        Unreviewed;       457 AA.
AC   A0A0G1W0H2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KKU75805.1};
DE   Flags: Fragment;
GN   ORFNames=UY01_C0004G0032 {ECO:0000313|EMBL:KKU75805.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWB1_47_6.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618749 {ECO:0000313|EMBL:KKU75805.1, ECO:0000313|Proteomes:UP000034879};
RN   [1] {ECO:0000313|EMBL:KKU75805.1, ECO:0000313|Proteomes:UP000034879}
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   -!- SIMILARITY: Belongs to the CapA family.
CC       {ECO:0000256|ARBA:ARBA00005662}.
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:KKU75805.1}.
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DR   EMBL; LCOJ01000004; KKU75805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1W0H2; -.
DR   Proteomes; UP000034879; 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: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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR019079; Capsule_synth_CapA.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR33393; POLYGLUTAMINE SYNTHESIS ACCESSORY PROTEIN RV0574C-RELATED; 1.
DR   PANTHER; PTHR33393:SF11; POLYGLUTAMINE SYNTHESIS ACCESSORY PROTEIN RV0574C-RELATED; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   Pfam; PF09587; PGA_cap; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SMART; SM00854; PGA_cap; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KKU75805.1};
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:KKU75805.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          338..457
FT                   /note="Capsule synthesis protein CapA"
FT                   /evidence="ECO:0000259|SMART:SM00854"
FT   ACT_SITE        104
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        107
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
FT   NON_TER         457
FT                   /evidence="ECO:0000313|EMBL:KKU75805.1"
SQ   SEQUENCE   457 AA;  49760 MW;  761B53FBFD44F033 CRC64;
     MKFVRKNKRI IVWAAFPVAF GVLVSSFLFS FLKIGNALEN TKNVLFAVSM APEENQSEKP
     QYFYINKSEG TKPKVSAQAF LVGDLKTGEV ILSKNQETKF PMASVSKLMT ALVTSELAKS
     EDVATVSKKA IATLGQNGEL RAGEKIKAAD LVYPLLLESS NDAAEALAEH FGRQNFMDKM
     NLQAEQLMMS STSYEDPSGL SPNNKSTAAD LFKLAGYIEE KHGELFDITA KRSYSAPKHN
     WSNISQFLGK DGYSGGKSGY TDAALQSGVA IFELPLGESG TRPIAITLLR SLDRKKDVEN
     ILKYLGSYVY YGGKTDSARA WVEEKVGMPP IYEPSFVTLS FLGDIMLDRG VRGSVVKNFK
     NDYSALFVKI PQKLLKNSDI AFANLEGTAS DQGVDGKNLY SFRMDPGVIP ALAGAGLDIL
     SVGNNHVGDW GRSAYADTLS RLKENEILYT GGGMGEA
//
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