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Database: UniProt/TrEMBL
Entry: Q7VBP1_PROMA
LinkDB: Q7VBP1_PROMA
Original site: Q7VBP1_PROMA 
ID   Q7VBP1_PROMA            Unreviewed;       466 AA.
AC   Q7VBP1;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   29-OCT-2014, entry version 86.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|RuleBase:RU004136};
DE            EC=6.3.2.10 {ECO:0000256|RuleBase:RU004136};
GN   Name=murF {ECO:0000313|EMBL:AAQ00096.1};
GN   OrderedLocusNames=Pro_1051 {ECO:0000313|EMBL:AAQ00096.1};
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539 {ECO:0000313|EMBL:AAQ00096.1, ECO:0000313|Proteomes:UP000001420};
RN   [1] {ECO:0000313|EMBL:AAQ00096.1, ECO:0000313|Proteomes:UP000001420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
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.
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.
CC   -!- SIMILARITY: Belongs to the MurCDEF family.
CC       {ECO:0000256|RuleBase:RU003630}.
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DR   EMBL; AE017126; AAQ00096.1; -; Genomic_DNA.
DR   RefSeq; NP_875443.1; NC_005042.1.
DR   ProteinModelPortal; Q7VBP1; -.
DR   STRING; 167539.Pro1051; -.
DR   EnsemblBacteria; AAQ00096; AAQ00096; Pro_1051.
DR   GeneID; 1462433; -.
DR   KEGG; pma:Pro_1051; -.
DR   PATRIC; 23028821; VBIProMar8617_1101.
DR   KO; K01929; -.
DR   OMA; PGNRNNE; -.
DR   OrthoDB; EOG6PKFCR; -.
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: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:0071555; P:cell wall organization; 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 {ECO:0000256|RuleBase:RU003630};
KW   Cell cycle {ECO:0000256|RuleBase:RU004136};
KW   Cell division {ECO:0000256|RuleBase:RU004136};
KW   Cell shape {ECO:0000256|RuleBase:RU004136};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004136};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001420};
KW   Ligase {ECO:0000256|RuleBase:RU003630};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003630};
KW   Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001420}.
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
//
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