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Database: UniProt/TrEMBL
Entry: A3PBY4_PROM0
LinkDB: A3PBY4_PROM0
Original site: A3PBY4_PROM0 
ID   A3PBY4_PROM0            Unreviewed;       457 AA.
AC   A3PBY4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   14-MAY-2014, entry version 56.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase;
DE            EC=6.3.2.10;
GN   Name=murF; OrderedLocusNames=P9301_06361;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- FUNCTION: Involved in cell wall formation. Catalyzes the final
CC       step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the
CC       precursor of murein (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-
CC       glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-
CC       acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC       alanine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the MurCDEF family.
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DR   EMBL; CP000576; ABO17259.1; -; Genomic_DNA.
DR   RefSeq; YP_001090860.1; NC_009091.1.
DR   ProteinModelPortal; A3PBY4; -.
DR   STRING; 167546.P9301_06361; -.
DR   EnsemblBacteria; ABO17259; ABO17259; P9301_06361.
DR   GeneID; 4911123; -.
DR   KEGG; pmg:P9301_06361; -.
DR   PATRIC; 22994867; VBIProMar103344_0622.
DR   eggNOG; COG0770; -.
DR   HOGENOM; HOG000268120; -.
DR   KO; K01929; -.
DR   OMA; ENITYAK; -.
DR   OrthoDB; EOG6PKFCR; -.
DR   BioCyc; PMAR167546:GH1Y-656-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.40.1390.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005863; UDP-N-AcMur-pentapeptide_synth.
DR   PANTHER; PTHR23135:SF3; PTHR23135:SF3; 1.
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;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Ligase;
KW   Nucleotide-binding; Peptidoglycan synthesis.
SQ   SEQUENCE   457 AA;  51592 MW;  9753AFDB74132804 CRC64;
     MDFSFFEIKD VLGDIKNLGE GGIDSLNFKN ICIDSRTCLK NDLFIAIKGK NFDGHNFLPD
     VLNKGVKSVV IKEGMQKLLP DNFPCWVVSD TLNAFQKLTL LKRKKLSIPV VAITGSVGKT
     TTKEMVGEVL NKLGKIKLSH ANFNNEIGVG LTILATDKED KVLVLEMGMR GLGQIENLSK
     YSKPDIAVIT NIGTAHIGLL GSKKNITYAK CEISKFLNPK GVVIIPANDL LLEETLREYW
     KGRVTKVELL NIENQNDSFK KDNNLRGFYN PSNKTILIEE NIFEISFEGF HNASNFLLAY
     AVAKELGIDF ESFNKFDFVS LGGRNKILKS VKTTIYDESY NASPESVKAC IKTLLEKPRN
     KFFIFGSMQE LGEESEKFHK EIFNLINNSD IEKCLFICDK KNKKIYTNYL KDKKKFLVLN
     NIKDVPKEIN KSTKKGDSIL IKGSRSWQLE KIIELIN
//
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