ID A0A061PHC2_9BACL Unreviewed; 248 AA.
AC A0A061PHC2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=D-alanine-D-alanine ligase {ECO:0000313|EMBL:GAK14266.1};
GN ORFNames=JCM19039_4170 {ECO:0000313|EMBL:GAK14266.1};
OS Geomicrobium sp. JCM 19039.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK14266.1, ECO:0000313|Proteomes:UP000027177};
RN [1] {ECO:0000313|EMBL:GAK14266.1, ECO:0000313|Proteomes:UP000027177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK14266.1,
RC ECO:0000313|Proteomes:UP000027177};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
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:GAK14266.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAXB01000029; GAK14266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061PHC2; -.
DR Proteomes; UP000027177; 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:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 2.
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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:GAK14266.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000027177}.
FT DOMAIN 9..209
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 106..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 248 AA; 26661 MW; 345581F536691C36 CRC64;
MVLWARMDED MEAVVTQVEE KLGYPAIVKP ANLGSSVGIG IARNRTSLET AVEEALEYAS
KLVIEPLIGE LKEINCSVLG DTEHAEASVL EEVLKTEEIL SYADKYQGSS NGGSKSSGGS
KGTSGGMEST DRIIPAPVSD ERTEEIQSLG VRTFKALGCG GVSRIDFMID ETNDSVYVNE
INTIPGSLSF YLWEPAGKDF QTLTHDMIQL ALKRQRDRER LTFSIDSNLF SLQGGGGGKG
GSKGGSKK
//
