(data stored in ACNUC7421 zone)

SWISSPROT: A8FQ96_SHESH

ID   A8FQ96_SHESH            Unreviewed;       455 AA.
AC   A8FQ96;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 76.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE            EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
GN   Name=murF {ECO:0000256|HAMAP-Rule:MF_02019};
GN   OrderedLocusNames=Ssed_0406 {ECO:0000313|EMBL:ABV35019.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35019.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35019.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35019.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
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. {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02019}.
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DR   EMBL; CP000821; ABV35019.1; -; Genomic_DNA.
DR   RefSeq; WP_012140756.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ96; -.
DR   STRING; 425104.Ssed_0406; -.
DR   EnsemblBacteria; ABV35019; ABV35019; Ssed_0406.
DR   KEGG; sse:Ssed_0406; -.
DR   eggNOG; ENOG4108EQQ; Bacteria.
DR   eggNOG; COG0770; LUCA.
DR   HOGENOM; HOG000268120; -.
DR   KO; K01929; -.
DR   OMA; SYNNHWG; -.
DR   OrthoDB; POG091H00FE; -.
DR   BioCyc; SSED425104:GH7Q-415-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   HAMAP; MF_02019; MurF; 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_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; A8FQ96.
DR   SWISS-2DPAGE; A8FQ96.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:ABV35019.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136}.
FT   DOMAIN       24     71       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      106    292       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      313    395       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     107    113       ATP. {ECO:0000256|HAMAP-Rule:MF_02019}.
SQ   SEQUENCE   455 AA;  48754 MW;  F1DD5D77ACDD8F7C CRC64;
     MIPLTLLQLS HRLDARLIGP DTEIAYVCSD SRSIPPQTLF VALKGERFDG HDFAHLAVEN
     GANALLVTHE LPLDLPQLIV KDTQKAMGEI GAYLREVIQP KSIALTGSNG KTSVKEMVAT
     ILSQRHKVLY TAGNFNNEIG VPLTLLRLEE GDEFGVFELG ANHRGEIDYT SSLVKPDVAL
     VNNVASAHLE GFGSLAGVAA AKSEIFNHLS PDGTAVINAD DSFARVMKEA ASEHKQLTFA
     IEAAADLQGS GLEPDLLGRY CFKMSYLNQE VSVTLPLSGR HQVSNALAAA GICLTLGLPL
     SEIVSGLSLL EPVKGRMLPT QLGRVRVIDD SYNANPASVS AAIDWLQEID GYRCLVLGDL
     GELGDNASLL HTELGELAKI RGIEALFSLG ELSANASTAF GGVHHQELEQ VVNNLVNHIN
     QLQGDVTVLV KGSRSAKMER VVEALIVAYG RGEFV
//

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