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Database: UniProt
Entry: A0A1G2N9Q5_9BACT
LinkDB: A0A1G2N9Q5_9BACT
Original site: A0A1G2N9Q5_9BACT 
ID   A0A1G2N9Q5_9BACT        Unreviewed;       462 AA.
AC   A0A1G2N9Q5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2928_01350 {ECO:0000313|EMBL:OHA32109.1};
OS   Candidatus Taylorbacteria bacterium RIFCSPLOWO2_01_FULL_45_15b.
OC   Bacteria; Candidatus Taylorbacteria.
OX   NCBI_TaxID=1802319 {ECO:0000313|EMBL:OHA32109.1, ECO:0000313|Proteomes:UP000176221};
RN   [1] {ECO:0000313|EMBL:OHA32109.1, ECO:0000313|Proteomes:UP000176221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHA32109.1}.
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DR   EMBL; MHRX01000053; OHA32109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2N9Q5; -.
DR   STRING; 1802319.A2928_01350; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000176221; 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   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   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..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..201
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   DOMAIN          221..379
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
SQ   SEQUENCE   462 AA;  51008 MW;  A9BB65339562385C CRC64;
     MHDYIDKNAF GFIVKFSAAL IFAFFSTTFA AKTAAVFFLS DTEVLPAPLI VVREEALPTT
     IQAVPKRSER SFAAGSLEDH VPSAGKFIGI DLVNMELRLY QNATLIGAHK ILSKGKPGSH
     WETPSGSYEV KTKEKNHFSS IGRVNMPYSM QFFGNFFIHG WPTYESGKEV GDGYSGGCIR
     LSTDDAETVF SFADLGTSLY IFDREEQIIS TLGLALSDSV ELASEAYLVA DIQSGEVVME
     SSAGAKMPVY AITKLMTAIV ANESISFDKE LALQDGEAFS ETFGIFPERM VVGDLLHLLL
     LNREVDSAST LERFYGKNNF VDWMNDKARA IGMRTARFAD TNGISKENVA SADDLFELSR
     YLYVKKSFIL GITRRPDKII EVAERQFIVL NEHPFVGDES FRGGIATDAQ EVGKQSMLTF
     FRVSVGAEKR LFVAILLGSE NAALETRRAI EEVRLATASN TF
//
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