MURC_PSEAE
ID MURC_PSEAE Reviewed; 480 AA.
AC Q9HW02; Q9RGR6;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; OrderedLocusNames=PA4411;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAO1293;
RX PubMed=10675598; DOI=10.1111/j.1574-6968.2000.tb08972.x;
RA El Zoeiby A., Sanschagrin F., Lamoureux J., Darveau A., Levesque R.C.;
RT "Cloning, over-expression and purification of Pseudomonas aeruginosa murC
RT encoding uridine diphosphate N-acetylmuramate: L-alanine ligase.";
RL FEMS Microbiol. Lett. 183:281-288(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA El-Sherbeini M., Azzolina B.;
RT "Pseudomonas aeruginosa murC gene encoding UDP-N-acetylmuramyl:L-alanine
RT ligase.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00046};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC Rule:MF_00046}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG48251.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF110740; AAF14862.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF306766; AAG48251.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG07799.1; -; Genomic_DNA.
DR PIR; D83094; D83094.
DR RefSeq; NP_253101.1; NC_002516.2.
DR RefSeq; WP_003094121.1; NZ_QZGE01000004.1.
DR PDB; 5VVW; X-ray; 2.30 A; A/B/C/D/E/F/G/H=16-322.
DR PDB; 6X9F; X-ray; 2.35 A; A/B/C/D/E/F/G/H=16-480.
DR PDB; 6X9N; X-ray; 2.25 A; A/B/C/D/E/F/G/H=16-480.
DR PDBsum; 5VVW; -.
DR PDBsum; 6X9F; -.
DR PDBsum; 6X9N; -.
DR AlphaFoldDB; Q9HW02; -.
DR SMR; Q9HW02; -.
DR STRING; 287.DR97_1589; -.
DR BindingDB; Q9HW02; -.
DR PaxDb; Q9HW02; -.
DR PRIDE; Q9HW02; -.
DR EnsemblBacteria; AAG07799; AAG07799; PA4411.
DR GeneID; 881283; -.
DR KEGG; pae:PA4411; -.
DR PATRIC; fig|208964.12.peg.4620; -.
DR PseudoCAP; PA4411; -.
DR HOGENOM; CLU_028104_2_2_6; -.
DR InParanoid; Q9HW02; -.
DR OMA; DITYQLR; -.
DR PhylomeDB; Q9HW02; -.
DR BioCyc; PAER208964:G1FZ6-4498-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002438; 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..480
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000182135"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:6X9N"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5VVW"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:6X9N"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:6X9N"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:6X9N"
SQ SEQUENCE 480 AA; 51982 MW; 228C595071D58FF6 CRC64;
MVKEPNGVTR TMRRIRRIHF VGIGGAGMCG IAEVLLNLGY EVSGSDLKAS AVTERLEKFG
AQIFIGHQAE NADGADVLVV SSAINRANPE VASALERRIP VVPRAEMLAE LMRYRHGIAV
AGTHGKTTTT SLIASVFAAG GLDPTFVIGG RLNAAGTNAQ LGASRYLVAE ADESDASFLH
LQPMVAVVTN IDADHMATYG GDFNKLKKTF VEFLHNLPFY GLAVMCVDDP VVREILPQIA
RPTVTYGLSE DADVRAINIR QEGMRTWFTV LRPEREPLDV SVNMPGLHNV LNSLATIVIA
TDEGISDEAI VQGLSGFQGV GRRFQVYGEL QVEGGSVMLV DDYGHHPREV AAVIKAIRGG
WPERRLVMVY QPHRYTRTRD LYEDFVQVLG EANVLLLMEV YPAGEEPIPG ADSRQLCHSI
RQRGQLDPIY FERDADLAPL VKPLLRAGDI LLCQGAGDVG GLAPQLIKNP LFAGKGGKGA
