ID A3PBY4_PROM0 Unreviewed; 457 AA.
AC A3PBY4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 01-MAY-2013, entry version 50.
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:E231-E231(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; NHKGEIR; -.
DR ProtClustDB; CLSK921907; -.
DR BioCyc; PMAR167546:GH1Y-681-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: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; 3.90.190.20; -; 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; Mur_ligase_C; 1.
DR SUPFAM; SSF53623; Mur_ligase_cen; 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
//
