ID   D2QK37_SPILD            Unreviewed;       551 AA.
AC   D2QK37;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=D-alanine--D-alanine ligase domain protein {ECO:0000313|EMBL:ADB37159.1};
GN   OrderedLocusNames=Slin_1108 {ECO:0000313|EMBL:ADB37159.1};
OS   Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896 / Claus 1).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB37159.1};
RN   [1] {ECO:0000313|EMBL:ADB37159.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 74 {ECO:0000313|EMBL:ADB37159.1};
RX   PubMed=21304700;
RA   Lail K., Sikorski J., Saunders E., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.-F., Lucas S., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA   Jeffries C.D., Chain P., Brettin T., Detter J.C., Schuetze A., Rohde M.,
RA   Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.-P., Chen F.;
RT   "Complete genome sequence of Spirosoma linguale type strain (1).";
RL   Stand. Genomic Sci. 2:176-185(2010).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP001769; ADB37159.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2QK37; -.
DR   STRING; 504472.Slin_1108; -.
DR   KEGG; sli:Slin_1108; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_489909_0_0_10; -.
DR   Proteomes; UP000002028; 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:InterPro.
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; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
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; 2.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADB37159.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          219..430
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   551 AA;  60944 MW;  B63B528D14BC5272 CRC64;
     MKIGIFFGGP AREREVSFAG GRTALANLDK GLFEPVLVFV DGRGRFRLVS PDFLQSPSLH
     DALPQDSSGF SVYDESLAVD TLDAILPELR PEQFRDHFDL AFLAMHGPDC EDGAIQGLLE
     WHKMPYTGPG LVGSAVGINK ILQNELIALA NGQKKKTATI SRDDYEQADK AQFFQSLVEH
     LGLPIVIKAP HQGSSIGVAI VREADLAQFC RSVEQCFFTM SIQPDGWSKL SGWTSLSGTE
     KHELAQKMVS LDSGISFPVV IEQTGEVIKH PADFVARLDA LMAQSSQPIT LASLNAEDEV
     LFEEFITGQE FSCGVIQDDD QVAIALPPTE IYNVTSFDFE SKYKLNTTKK RIPVETSLEN
     NRKIQLAVAQ VFTRLGINVY SRIDGFLTPA GDVLLHDPNT IPGMSPSSLI FKQMAEIGLN
     LANSLTYLIR QSLRERIRTG KDTFHLKHLL AELDAQLAHR KANPLPERVV SFGSGDEEFI
     AAKQQYNELA ASGTVRPSLM YIKSKQESHE IPVNLLFKDT IAELETALSQ PRHPLLLETA
     ELARHITERY V
//