ID A7GYC3_CAMC5 Unreviewed; 347 AA.
AC A7GYC3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:EAT99804.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:EAT99804.1};
GN Name=ddlA {ECO:0000313|EMBL:EAT99804.1};
GN ORFNames=CCV52592_1152 {ECO:0000313|EMBL:EAT99804.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:EAT99804.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP000767; EAT99804.1; -; Genomic_DNA.
DR RefSeq; WP_011992262.1; NC_009715.2.
DR AlphaFoldDB; A7GYC3; -.
DR STRING; 360105.CCV52592_1152; -.
DR KEGG; ccv:CCV52592_1152; -.
DR HOGENOM; CLU_039268_0_2_7; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000006380; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; 3.40.50.20; -; 1.
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; IPR005905; D_ala_D_ala.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAT99804.1};
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:UP000006380}.
FT DOMAIN 133..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 347 AA; 39781 MW; F26A795969764B80 CRC64;
MKLGVVFGAK SFEHEISIVS AIVLKNVLKQ ELSFIFCDKE RKFYLIEPTD MRANFFSSGK
YKKCKKLFLM ACGFYTHSLF GVKRLEVDVY INLIHGMDGE DGKFASLFDF YGISYIGPRL
EASVMSYNKE LTKFLAQKVG VKTLDYEMIT YEELPKFALP IILKPARLGS SIGVSVVKDE
SEFEYARDVA FEFDKEVLVE PFIEGVKEYN LAGCMIDGKM RFSIVEEPKK KEFLDYEQKY
MSFSNESKAQ EARIDEELRD RLKENFVKIY GFGFEGAIIR CDFFVIEGEV YLNEINPNPG
SLANYLFEDF EAMLNALAAS RLPKERKINI DYKFINSITS AKGSGKI
//
