MURC_HAEIN
ID MURC_HAEIN Reviewed; 475 AA.
AC P45066;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
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=HI_1139;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22794.1; -; Genomic_DNA.
DR PIR; E64185; E64185.
DR RefSeq; NP_439297.1; NC_000907.1.
DR RefSeq; WP_005693453.1; NC_000907.1.
DR PDB; 1GQQ; X-ray; 3.10 A; A/B=1-475.
DR PDB; 1GQY; X-ray; 1.80 A; A/B=1-475.
DR PDB; 1P31; X-ray; 1.85 A; A/B=1-475.
DR PDB; 1P3D; X-ray; 1.70 A; A/B=1-475.
DR PDBsum; 1GQQ; -.
DR PDBsum; 1GQY; -.
DR PDBsum; 1P31; -.
DR PDBsum; 1P3D; -.
DR AlphaFoldDB; P45066; -.
DR SMR; P45066; -.
DR STRING; 71421.HI_1139; -.
DR DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR DrugBank; DB01673; Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine.
DR EnsemblBacteria; AAC22794; AAC22794; HI_1139.
DR KEGG; hin:HI_1139; -.
DR PATRIC; fig|71421.8.peg.1189; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_6; -.
DR OMA; DITYQLR; -.
DR PhylomeDB; P45066; -.
DR BioCyc; HINF71421:G1GJ1-1172-MON; -.
DR BRENDA; 6.3.2.8; 2529.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P45066; -.
DR Proteomes; UP000000579; 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..475
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000182100"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1GQY"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1GQQ"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1P3D"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 440..447
FT /evidence="ECO:0007829|PDB:1P3D"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:1P3D"
FT HELIX 462..472
FT /evidence="ECO:0007829|PDB:1P3D"
SQ SEQUENCE 475 AA; 51994 MW; 5748EDD753D6F8D3 CRC64;
MKHSHEEIRK IIPEMRRVQQ IHFIGIGGAG MSGIAEILLN EGYQISGSDI ADGVVTQRLA
QAGAKIYIGH AEEHIEGASV VVVSSAIKDD NPELVTSKQK RIPVIQRAQM LAEIMRFRHG
IAVAGTHGKT TTTAMISMIY TQAKLDPTFV NGGLVKSAGK NAHLGASRYL IAEADESDAS
FLHLQPMVSV VTNMEPDHMD TYEGDFEKMK ATYVKFLHNL PFYGLAVMCA DDPVLMELVP
KVGRQVITYG FSEQADYRIE DYEQTGFQGH YTVICPNNER INVLLNVPGK HNALNATAAL
AVAKEEGIAN EAILEALADF QGAGRRFDQL GEFIRPNGKV RLVDDYGHHP TEVGVTIKAA
REGWGDKRIV MIFQPHRYSR TRDLFDDFVQ VLSQVDALIM LDVYAAGEAP IVGADSKSLC
RSIRNLGKVD PILVSDTSQL GDVLDQIIQD GDLILAQGAG SVSKISRGLA ESWKN
