ID Q7VBP1_PROMA Unreviewed; 466 AA.
AC Q7VBP1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 78.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase;
DE EC=6.3.2.10;
GN Name=murF; OrderedLocusNames=Pro_1051;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F.,
RA Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B.,
RA Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P.,
RA Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120,
RT a nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00096.1; -; Genomic_DNA.
DR RefSeq; NP_875443.1; NC_005042.1.
DR HSSP; P11880; 1GG4.
DR ProteinModelPortal; Q7VBP1; -.
DR STRING; 167539.Pro1051; -.
DR EnsemblBacteria; AAQ00096; AAQ00096; Pro_1051.
DR GeneID; 1462433; -.
DR KEGG; pma:Pro1051; -.
DR PATRIC; 23028821; VBIProMar8617_1101.
DR KO; K01929; -.
DR OMA; HIGQLKT; -.
DR ProtClustDB; CLSK919513; -.
DR BioCyc; PMAR167539:GJN2-1078-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; Reference proteome.
SQ SEQUENCE 466 AA; 51421 MW; 194CD6C1FB48DFA5 CRC64;
MVLRLLNLND IWGPPYQNKL VNLDAPLGTV CTDSRNIKKG NFFVPLIGNK FDGHLFLEEV
FEKGVQAAFI SKDCNLAIPE ELLYWQVDDT QEAYQKLAFL HRRLFSIPVV AVTGSAGKTT
TRELIHSSLV PLGEVLATSN NNNNDIGVPF TLLKANVNHS AIVLEMAMRG LGQIERLSKC
ACPDIAVITN IGSSHIGLLG SKQNIASAKC EIAAHMNPNG FVIIPAGDQL LEKTLQEVWK
GRIVRVDIES KSNPFFANEY DSHQTKKNVD YLGVLDSDNW QITYDGIIFQ MPLQGRHNAI
NFMFALAVAY ELNVPLDSIR NLSVNLPPGR NHSLTFGNIN VLDETYNASP ESVIASLDLL
ATKPGRHFAV LGNMYELGEK TIDYHEQIVQ HSIATGLTGL VICVNGPEAE AMLLAGQPLS
YIEVVSTPED AFLILKSWLN SGDYLLLKAS RKVSLERILP LLKEAY
//
