ID A0A1F6W7T6_9BACT Unreviewed; 415 AA.
AC A0A1F6W7T6;
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=A3D42_00470 {ECO:0000313|EMBL:OGI77894.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_02_FULL_41_18.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801754 {ECO:0000313|EMBL:OGI77894.1, ECO:0000313|Proteomes:UP000177777};
RN [1] {ECO:0000313|EMBL:OGI77894.1, ECO:0000313|Proteomes:UP000177777}
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:OGI77894.1}.
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DR EMBL; MFUE01000008; OGI77894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6W7T6; -.
DR STRING; 1801754.A3D42_00470; -.
DR Proteomes; UP000177777; 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; 2.
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; 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 12..112
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 117..214
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 277..354
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 415 AA; 46567 MW; E04DC075A09B90CB CRC64;
MSLDYFSTIK KIFFIGIGGI GISALAKMVS SRGIEVSGVN DEESPKTLNP LRELGAEIFR
LDQVKAELPE ADLYVYSDAW IYREPEILKK ARTTDKPVLS YFEALGEFAK EYKVIAISGT
HGKTTTTAMV AGILVDAGLD PTVIVGSFVK KFNSNFRPGK SEWFVIEADE YNRHFLNFHP
YIGVVTNIEA DHLDYYKDLD DIKNAFKQFI LQSEIAISDY SKYLDKVPKL SVPGEHNRQN
AAAALSVADI LKIPETLAQK SLAEFSGTWR RLEKRAETKE GTIIYDDYAH HPTEIRASLH
ALRELYPKKK ITIVFQPHLY SRTKALFGDF TLSFGDAEKV LFLPIYFARE DNDESVSSHK
LAQAVRLQGV DAEAMPDFEI TEAYVKTLNL GKNDVFVTMG AGEAYKVADK VFNLA
//
