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Database: UniProt
Entry: A0A0W0SLS5_9GAMM
LinkDB: A0A0W0SLS5_9GAMM
Original site: A0A0W0SLS5_9GAMM 
ID   A0A0W0SLS5_9GAMM        Unreviewed;       453 AA.
AC   A0A0W0SLS5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000313|EMBL:KTC84185.1};
GN   ORFNames=Lbru_1546 {ECO:0000313|EMBL:KTC84185.1};
OS   Legionella brunensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC84185.1, ECO:0000313|Proteomes:UP000054742};
RN   [1] {ECO:0000313|EMBL:KTC84185.1, ECO:0000313|Proteomes:UP000054742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC84185.1,
RC   ECO:0000313|Proteomes:UP000054742};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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:KTC84185.1}.
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DR   EMBL; LNXV01000011; KTC84185.1; -; Genomic_DNA.
DR   RefSeq; WP_058441612.1; NZ_LNXV01000011.1.
DR   AlphaFoldDB; A0A0W0SLS5; -.
DR   STRING; 29422.Lbru_1546; -.
DR   PATRIC; fig|29422.6.peg.1636; -.
DR   OrthoDB; 9804126at2; -.
DR   Proteomes; UP000054742; 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; IPR005757; Mpl.
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   NCBIfam; TIGR01081; mpl; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 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; 1.
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:KTC84185.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   DOMAIN          2..99
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          108..292
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          313..381
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   453 AA;  49990 MW;  DF3A5028900FEBC1 CRC64;
     MHLHILGISG TFMSALAILA REAGFKVTGC DANCYPPVSD LLRAKDIEWT EGYDDSTLAL
     KADCVIVGNA IKRGMPVLEA VLNAGKNYTS GPQWLAENIL PRYRVLAVAG THGKTTTTSM
     LAFILQQAGL QPGFLIGGVA PNFNTSAYLG QGQWFVIEAD EYDSAFFDKR PKLMHYRPEV
     AILNNLEFDH ADIYANLEAI QQQFHYYLKT IPGKGVVIKP RDDAALNKVL MQGVFSPVEE
     LALNGDATWR AEIRDESGRS FCVWHKGKAV AEVNWPLIGQ FNIENGLAAI AASYHAGVEI
     EVAARALAEF KPVKRRLEVK SNRYDITVYD DFAHHPTAIT KTINALKQSN RHKRILAVLE
     FASYTMKTGV HANAMAQALS TVDCAYVLNP EHFSLSNVVK DWVCPYQVLP NANAIVSAVV
     AEARPGDAIL VMSNRGFDNI HQHLVSYIDL KFK
//
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