(data stored in ACNUC7421 zone)

SWISSPROT: MURF_BACSU

ID   MURF_BACSU              Reviewed;         457 AA.
AC   P96613;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 133.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02019};
DE            EC=6.3.2.10 {ECO:0000255|HAMAP-Rule:MF_02019};
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_02019};
DE   AltName: Full=UDP-MurNAc-pentapeptide synthetase;
GN   Name=murF {ECO:0000255|HAMAP-Rule:MF_02019}; Synonyms=ydbQ;
GN   OrderedLocusNames=BSU04570;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in
CC       the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of
CC       murein. {ECO:0000255|HAMAP-Rule:MF_02019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC         alanyl-gamma-D-glutamyl-L-lysine = ADP + H(+) + phosphate + UDP-N-
CC         acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC         alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57822, ChEBI:CHEBI:70758,
CC         ChEBI:CHEBI:83903, ChEBI:CHEBI:456216; EC=6.3.2.10;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02019};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02019}.
DR   EMBL; AB001488; BAA19294.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12264.1; -; Genomic_DNA.
DR   PIR; F69662; F69662.
DR   RefSeq; NP_388338.1; NC_000964.3.
DR   RefSeq; WP_003246696.1; NZ_JNCM01000031.1.
DR   SMR; P96613; -.
DR   STRING; 224308.BSU04570; -.
DR   jPOST; P96613; -.
DR   PaxDb; P96613; -.
DR   PRIDE; P96613; -.
DR   EnsemblBacteria; CAB12264; CAB12264; BSU04570.
DR   GeneID; 939947; -.
DR   KEGG; bsu:BSU04570; -.
DR   PATRIC; fig|224308.179.peg.485; -.
DR   eggNOG; ENOG4107EES; Bacteria.
DR   eggNOG; COG0770; LUCA.
DR   HOGENOM; HOG000268119; -.
DR   InParanoid; P96613; -.
DR   KO; K01929; -.
DR   OMA; SYNNHWG; -.
DR   PhylomeDB; P96613; -.
DR   BioCyc; BSUB:BSU04570-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-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_02019; MurF; 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; IPR035911; MurE/MurF_N.
DR   InterPro; IPR005863; UDP-N-AcMur_synth.
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   SUPFAM; SSF63418; SSF63418; 1.
DR   TIGRFAMs; TIGR01143; murF; 1.
PE   3: Inferred from homology;
DR   PRODOM; P96613.
DR   SWISS-2DPAGE; P96613.
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..457
FT                   /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT                   ligase"
FT                   /id="PRO_0000101694"
FT   NP_BIND         113..119
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   457 AA;  49723 MW;  5BC1D62048AA958A CRC64;
     MIKRTVKNIA EMVKGTLANP QYEQTVIHGV ATDTRKLEQH QLFIPLKGER FDGHSFVEQA
     FEAGVAAVLW DRSVPNPPEN HAVILVDDTL TALQQLAKAY LQELGTRVIG VTGSNGKTTT
     KDMIHAVLGT QYRVHKTGGN FNNHIGLPLT VLAMPENTEI AVLEMGMSAK GEIDLLSRLA
     NPDAAVITNI GESHMQDLGS REGIAEAKLE IINGLKEDGV LIYIGDEPLL QNAYSCQTKT
     YGTGTHNDYQ LQDVSQSEEG THFTIKGIEN TFFIPILGKH NVMNAMAAIA AGAYFGIAPE
     DAAKGLSGLK VTGMRLELIK TDSGLSIIND AYNASPTSMK AAIQLTESLE GYGKKMLVLG
     DMLELGDLEE TFHKECGAVI SPDKIDRVFT YGKLGAFIAE GALKHFEKDR VSHYTEKKDL
     LQAVKENASK GDLILFKASR GMKLEEIVKD LIESPLS
//

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