ID K2FQH0_9BACT Unreviewed; 219 AA.
AC K2FQH0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=ACD_5C00305G0002 {ECO:0000313|EMBL:EKE25078.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE25078.1};
RN [1] {ECO:0000313|EMBL:EKE25078.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKE25078.1}.
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DR EMBL; AMFJ01001313; EKE25078.1; -; Genomic_DNA.
DR AlphaFoldDB; K2FQH0; -.
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:SF25; D-ALANINE--D-ALANINE LIGASE A; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 7..210
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 219 AA; 24933 MW; 7A095208EF56CA55 CRC64;
MDKDVAKRLL NEAGFKQAKF HVIKKEDKYE NKINGIIKDL KFPIFVKPAR QGSSVGISKV
WKRNDLLNAI QEAFKFDSKI ILEQAIVGRE IECAVLGNAQ PVASDLGEIC LTNGFYSYDA
KYINENTACA IVNVKMSSIM KKRIRETAIN IYKTLECEGM SRVDFFLTEK NEIYINEINT
LPGFTDVSMY PKLMEISGIN YPILLESLID FAIEKRNKN
//
