MURC_THEMA
ID MURC_THEMA Reviewed; 457 AA.
AC Q9WY73;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase;
DE EC=6.3.2.8;
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase;
GN Name=murC; OrderedLocusNames=TM_0231;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=15146505; DOI=10.1002/prot.20034;
RA Spraggon G., Schwarzenbacher R., Kreusch A., Lee C.C., Abdubek P.,
RA Ambing E., Biorac T., Brinen L.S., Canaves J.M., Cambell J., Chiu H.-J.,
RA Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., Eshagi S., Floyd R.,
RA Godzik A., Grittini C., Grzechnik S.K., Hampton E., Jaroszewski L.,
RA Karlak C., Klock H.E., Koesema E., Kovarik J.S., Kuhn P., Levin I.,
RA McMullan D., McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J.,
RA Page R., Quijano K., Robb A., Stevens R.C., van den Bedem H., Velasquez J.,
RA Vincent J., von Delft F., Wang X., West B., Wolf G., Xu Q., Hodgson K.O.,
RA Wooley J., Lesley S.A., Wilson I.A.;
RT "Crystal structure of an UDP-N-acetylmuramate-alanine ligase MurC (TM0231)
RT from Thermotoga maritima at 2.3-A resolution.";
RL Proteins 55:1078-1081(2004).
CC -!- FUNCTION: Cell wall formation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35322.1; -; Genomic_DNA.
DR PIR; A72402; A72402.
DR RefSeq; NP_228045.1; NC_000853.1.
DR RefSeq; WP_004082924.1; NZ_CP011107.1.
DR PDB; 1J6U; X-ray; 2.30 A; A=1-457.
DR PDBsum; 1J6U; -.
DR AlphaFoldDB; Q9WY73; -.
DR SMR; Q9WY73; -.
DR STRING; 243274.THEMA_03570; -.
DR EnsemblBacteria; AAD35322; AAD35322; TM_0231.
DR KEGG; tma:TM0231; -.
DR eggNOG; COG0773; Bacteria.
DR InParanoid; Q9WY73; -.
DR OMA; DITYQLR; -.
DR OrthoDB; 307881at2; -.
DR BRENDA; 6.3.2.8; 6331.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q9WY73; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR HAMAP; MF_00046; MurC; 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 InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01082; murC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..457
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000182177"
FT BINDING 109..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1J6U"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1J6U"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 226..238
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:1J6U"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:1J6U"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:1J6U"
FT HELIX 431..445
FT /evidence="ECO:0007829|PDB:1J6U"
SQ SEQUENCE 457 AA; 51872 MW; 7D9AEDC50482351D CRC64;
MKIHFVGIGG IGMSAVALHE FSNGNDVYGS NIEETERTAY LRKLGIPIFV PHSADNWYDP
DLVIKTPAVR DDNPEIVRAR MERVPIENRL HYFRDTLKRE KKEEFAVTGT DGKTTTTAMV
AHVLKHLRKS PTVFLGGIMD SLEHGNYEKG NGPVVYELDE SEEFFSEFSP NYLIITNARG
DHLENYGNSL TRYRSAFEKI SRNTDLVVTF AEDELTSHLG DVTFGVKKGT YTLEMRSASR
AEQKAMVEKN GKRYLELKLK VPGFHNVLNA LAVIALFDSL GYDLAPVLEA LEEFRGVHRR
FSIAFHDPET NIYVIDDYAH TPDEIRNLLQ TAKEVFENEK IVVIFQPHRY SRLEREDGNF
AKALQLADEV VVTEVYDAFE EKKNGISGKM IWDSLKSLGK EAYFVEKLPE LEKVISVSEN
TVFLFVGAGD IIYSSRRFVE RYQSSKSSPS RVLGSNK
