ID A0A1F8E8R6_9BACT Unreviewed; 467 AA.
AC A0A1F8E8R6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2817_01495 {ECO:0000313|EMBL:OGM97182.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_01_FULL_39_8b.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802659 {ECO:0000313|EMBL:OGM97182.1, ECO:0000313|Proteomes:UP000177594};
RN [1] {ECO:0000313|EMBL:OGM97182.1, ECO:0000313|Proteomes:UP000177594}
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 -!- 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:OGM97182.1}.
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DR EMBL; MGIZ01000058; OGM97182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8E8R6; -.
DR Proteomes; UP000177594; 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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 4..98
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 111..294
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 315..393
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 467 AA; 51719 MW; D8BCCF94E405EA35 CRC64;
MKKKVYFLGI GGIAMANLAC LLKQKDFLVS GSDLDTFGPS AELLKKHKIN YFKDHDPNHI
KKFKPDITVV GNAIKRGNQG LEYILDNQIA HCSMPEIIKT EIIRDKKSIV ITGTSGKTTT
TALIALVLYK AGLKPTALIG GIVKNLDSGF INGNSSYTVI EGDEYGSSYN DNSPKFIHYR
PYIALINNIQ PDHLDIYSSL EEIIKAFRKL PRLIPKKGLL VLNTGDKNSA ILKNDAKCKV
ETFGEGGVVT AKNIKTGPNG LDFELYRKNN LLGKIKTGLL GKHNVENILA ASTIALHIGI
SFKKLAEAVA MFKGVKRRLE IIYQKNNIKI IDDFAHNPDK VLASLSALRN HFSKHQIIAI
FEPRTGSSRR KFFQEAYISS FKPADLVYIA EPYKKSALSK EEMFSSQKLV KDLNKEGIKS
YALENADGII AHIKANYLKT NASPTIFCIM TSGDFDSIHQ KLVALVS
//
