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Database: UniProt
Entry: A0A1F6K708_9BACT
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ID   A0A1F6K708_9BACT        Unreviewed;       419 AA.
AC   A0A1F6K708;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A3B53_02475 {ECO:0000313|EMBL:OGH42889.1};
OS   Candidatus Levybacteria bacterium RIFCSPLOWO2_01_FULL_42_15.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1798626 {ECO:0000313|EMBL:OGH42889.1, ECO:0000313|Proteomes:UP000177490};
RN   [1] {ECO:0000313|EMBL:OGH42889.1, ECO:0000313|Proteomes:UP000177490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|RuleBase:RU004135}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|ARBA:ARBA00005898}.
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:OGH42889.1}.
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DR   EMBL; MFOZ01000019; OGH42889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6K708; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000177490; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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-UniPathway.
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   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; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   NCBIfam; TIGR01085; murE; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|RuleBase:RU004135};
KW   Cell division {ECO:0000256|RuleBase:RU004135};
KW   Cell shape {ECO:0000256|RuleBase:RU004135};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..218
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          241..319
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   419 AA;  46321 MW;  EFCDE95BDF21A6A7 CRC64;
     MWQEIKNVYH LLVAVAAQVW FGFPSRKLKV IGVTGTDGKT TTVNLIYHIL HTCGYSVSMI
     STVGAIINGE KKDLGFHVTN PSSWQLNSFI KKAAEKSSYL VLEVTSHGID QHRIFGIPFA
     IGVMTNVTNE HLDYHKTYDR YLQTKVKLLK RSRIAIVNQD DGSHKAIMLL LKDGNRMDRK
     VITYGKTKSP MVNPLVYAFK TKLIGNFNRS NEGAAIATVL ALNVKESCIK AACESFEAPI
     GRQQVVYEGD FTVMIDFAHT PNAIEEFLHS IKPGVKGRLI HVFGSAGERD RKKRPEMGKA
     SANYSDVIIL TAEDPRSESV AKIINEIESG IVNNSKFPGL APRSLAKGGR SGTGKIQSAK
     LFKISNRQEA INTAIKIAQK GDFVLVTGKG HEKSMNFGRG EIPWSEYDSV KEALVARKL
//
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