ID   V6I203_9LEPT            Unreviewed;       522 AA.
AC   V6I203;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Mur ligase family, glutamate ligase domain protein {ECO:0000313|EMBL:EQA64245.1};
GN   ORFNames=LEP1GSC062_2740 {ECO:0000313|EMBL:EQA64245.1};
OS   Leptospira alexanderi serovar Manhao 3 str. L 60.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049759 {ECO:0000313|EMBL:EQA64245.1, ECO:0000313|Proteomes:UP000018747};
RN   [1] {ECO:0000313|EMBL:EQA64245.1, ECO:0000313|Proteomes:UP000018747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L 60 {ECO:0000313|EMBL:EQA64245.1,
RC   ECO:0000313|Proteomes:UP000018747};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   Fouts D.E.;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:EQA64245.1}.
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DR   EMBL; AHMT02000009; EQA64245.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6I203; -.
DR   STRING; 100053.GCA_002009845_01337; -.
DR   Proteomes; UP000018747; Unassembled WGS sequence.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 2.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EQA64245.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          8..104
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          109..238
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          380..465
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   522 AA;  57119 MW;  B7B315C8FB77D4E1 CRC64;
     MSFQKPFFLG IGGSGMSSLA FLLLSKGLKV GGYDGKHSAV VEKLVLNGAT VLHKSDVLEA
     ENYDLAVYSS AIRLDSHPLV KKFKDKGIPL VHRSELLHQV MSEKKQISVA GSHGKTTTSA
     MTAFLLEKCG MSPSIMVGGE VAFLGGKGGS WGEGEWGIFE SDESDGTFNN HNAGIRILTN
     VDEDHLDHYQ TRENLLNAFA RYMERASRKL ILNLDDIGIR DSLTLIQDHS KILGFSKSFV
     SGGIANGLSQ NSDVEGTRTG DSDVAENRVI SSNLENETLR TGKKDISQYS KEKISSIETF
     GVRNNTGNDA LSDINSSKII YYTIESGSLS FRFQEKEYSF SLKYPGEHYL KNALAAILAC
     SEAGAPIAEL VSKISEYSGV SRRLEYLGSK NGIEVYDDYG HHPTEIKAVI QSMEGLKKNG
     RAIILFQPHR YTRTQNLYKE FAESLDTGES VYLLPIYPAG EDPIEGVGTE LISDSMKVPA
     KILPKEISEG IFTLKNSLKP GDKLITLGAG NVRDWGLAFL KD
//