(data stored in SCRATCH3701 zone)

SWISSPROT: MURC_SYNS3

ID   MURC_SYNS3              Reviewed;         483 AA.
AC   Q0IE55;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 97.
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=sync_0028;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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}.
DR   EMBL; CP000435; ABI46504.1; -; Genomic_DNA.
DR   RefSeq; WP_011618019.1; NC_008319.1.
DR   SMR; Q0IE55; -.
DR   STRING; 64471.sync_0028; -.
DR   PRIDE; Q0IE55; -.
DR   EnsemblBacteria; ABI46504; ABI46504; sync_0028.
DR   KEGG; syg:sync_0028; -.
DR   eggNOG; ENOG4105DFU; Bacteria.
DR   eggNOG; COG0773; LUCA.
DR   HOGENOM; HOG000256031; -.
DR   KO; K01924; -.
DR   OMA; DITYQLR; -.
DR   OrthoDB; 307881at2; -.
DR   BioCyc; SSP64471:G1G72-28-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001961; 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   3: Inferred from homology;
DR   PRODOM; Q0IE55.
DR   SWISS-2DPAGE; Q0IE55.
KW   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..483
FT                   /note="UDP-N-acetylmuramate--L-alanine ligase"
FT                   /id="PRO_1000004431"
FT   NP_BIND         122..128
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
SQ   SEQUENCE   483 AA;  52297 MW;  CC010133987A4498 CRC64;
     MADSIQPEKH IHFIGMGGIG MSALALILAE RGHSVSGSDR KLTPAMQALE TKALAIFESQ
     VSKNFAHLQS RGIEEPLVVV STAIPSTNPE LIEAQRLDLT IWHRSDLLAW LIEQQPSIAV
     AGSHGKTTTS TVLTTLLATV GEDPTAVIGG VVPCYGSNGH KGNGRLLVAE ADESDGSLVK
     FKASLGIITN LELDHTDHYR NLDDLIETMK TFGRGCKRLL INHDDPILKE HFQADACWSV
     HHVETADYAA LPVQLDGDRT IADYFEQGQK VGQITLPLPG LHNLSNVVAA LAACRMEGVP
     LEALLLAVTE LRSPGRRFDF RGEWQDRQVV DDYAHHPSEV QATLTMAQLM VQSGRSPLPR
     TPQRLLAVFQ PHRYSRTQEF LNAFAQALVS ADALVLAPIY GAGEQPIEGI NSELLARSIR
     LIDPNQPVFV ASTMEELAGL VKQHSQPDDL ILAMGAGDVN SLWERLSQEG IGGEASCSPA
     IAA
//

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