MURC_TRIEI
ID MURC_TRIEI Reviewed; 539 AA.
AC Q10XH7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=Tery_4029;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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=ABG53047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000393; ABG53047.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044136935.1; NC_008312.1.
DR AlphaFoldDB; Q10XH7; -.
DR SMR; Q10XH7; -.
DR STRING; 203124.Tery_4029; -.
DR EnsemblBacteria; ABG53047; ABG53047; Tery_4029.
DR KEGG; ter:Tery_4029; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_2_3; -.
DR OrthoDB; 307881at2; -.
DR UniPathway; UPA00219; -.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis.
FT CHAIN 1..539
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_0000336875"
FT BINDING 165..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ SEQUENCE 539 AA; 59675 MW; 6C31C1440990A39A CRC64;
MSKYVDLTGK PFHFIGIGGI GMSALAYILA KRKLPTYGSD IKSSHITRRL EAIGAHIFWH
QEAKNLELFQ QTTEEQNLFL SNNSSLNLSQ FTPCISLGEV TTKKHNVKLE NHKGISQLPQ
VVCSTAINTT NSEYKAAVEL GCPIFHRSDL LAALIQDYQS IAVAGTHGKT TTSSLIGFML
LEAGLDPTIV IGGEVDAWGG NARLGRSPYL VAEADESDGS LVKLSAHIGV VTNIELDHPD
HYDSLDQVVE IFQVFKENCQ NLVGCIDCST VREKLQPTIS YSINFESDAH YKVDCVHYQS
NVTLARVWEK GQILGQLKLR LLGKHNLSNA LAAVAVGRLL GLEFSTITSA IALFEGAHRR
FEYRGECNGI VFVDDYAHHP SEINATLAAA NLQKNQELSP KPHISTKKLT LKTQNNSLKI
ERVVAIFQPH RYSRTQAFIS EFAQSFNDAD MVIVTNIYSA GESSEGQINS QQVAEAISRY
HRQVYYRSSL DSVSKFLYQV LKPGDLAIFL SAGNLNQIIP ELMARYQQPH YQVKSCEIA