ID A0A1F6BG86_9BACT Unreviewed; 334 AA.
AC A0A1F6BG86;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=A2363_03655 {ECO:0000313|EMBL:OGG35792.1};
OS Candidatus Gottesmanbacteria bacterium RIFOXYB1_FULL_47_11.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798401 {ECO:0000313|EMBL:OGG35792.1, ECO:0000313|Proteomes:UP000176186};
RN [1] {ECO:0000313|EMBL:OGG35792.1, ECO:0000313|Proteomes:UP000176186}
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 -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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:OGG35792.1}.
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DR EMBL; MFKE01000005; OGG35792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6BG86; -.
DR STRING; 1798401.A2363_03655; -.
DR Proteomes; UP000176186; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR000291; D-Ala_lig_Van_CS.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 111..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 334 AA; 37583 MW; 111090960CBA8D83 CRC64;
MNIAVLYSVP TKRATNTPYV ETDTDTTESA KEIETALAVK GATVTTHPID EDHISSISDI
RADVIFNLIE WTGHDLPLAD RAFAAIEQTG IPFTGGNRHN YMMTSDKVSM KKALDAHALP
TARWQLFEDP GQPIRTDFRF PVIVKPALEH CSIGLSRDSI VSGAEKLRRK VREMIRALAQ
PMLIEEFITG REFQVTALEG PKGLRVLPPA EVVFDSADPN HMLTYASRWD ENDPEYKSSH
MKMTHIDQPL VREMERLTRR TFEKLGFRDY TRLDIRTRGN DVLILEANSN PGISDSDDYG
MTLSYKAVGW TLADFVWEIV ASAQRRGVKS HPPA
//
