ID Q4JVS1_CORJK Unreviewed; 202 AA.
AC Q4JVS1;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Putative D-alanine-D-alanine ligase {ECO:0000313|EMBL:CAI37086.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:CAI37086.1};
GN Name=ddlA1-C {ECO:0000313|EMBL:CAI37086.1};
GN OrderedLocusNames=jk0922 {ECO:0000313|EMBL:CAI37086.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI37086.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI37086.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI37086.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CR931997; CAI37086.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4JVS1; -.
DR STRING; 306537.jk0922; -.
DR KEGG; cjk:jk0922; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_3_1_11; -.
DR Proteomes; UP000000545; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:CAI37086.1};
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:UP000000545}.
FT DOMAIN 19..196
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 202 AA; 22234 MW; 871FCE938EBEA690 CRC64;
MARSLFSPKN RELTEDEQQR LGLPVFVKPA RRGSSIGISK VDSWEAFAQA VEIAFDHDNK
MIVESMIHGR EVECGVLQYP EGSVIASAPA MLEGTEDGDE GFYGFDAKYL DNTVTPSIPA
PIGEEATAEV RRLAVRTFEA LNCEGLARVD FFVTDNGEVI LNEINTLPGF TPISMYPQMF
IAGGMEYPQL LDILIARALV QD
//
