(data stored in SCRATCH zone)

SWISSPROT: A4ATW2_MARSH

ID   A4ATW2_MARSH            Unreviewed;       425 AA.
AC   A4ATW2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
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=FB2170_17396 {ECO:0000313|EMBL:EAR00882.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00882.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00882.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:
CC       Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-
CC         L-alanyl-gamma-D-glutamyl-L-lysine = ADP + H(+) + phosphate +
CC         UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-
CC         D-alanyl-D-alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57822,
CC         ChEBI:CHEBI:70758, ChEBI:CHEBI:83903, ChEBI:CHEBI:456216;
CC         EC=6.3.2.10; Evidence={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; CP002157; EAR00882.1; -; Genomic_DNA.
DR   RefSeq; WP_013304685.1; NC_014472.1.
DR   STRING; 313603.FB2170_17396; -.
DR   EnsemblBacteria; EAR00882; EAR00882; FB2170_17396.
DR   KEGG; fbc:FB2170_17396; -.
DR   eggNOG; ENOG4107EES; Bacteria.
DR   eggNOG; COG0770; LUCA.
DR   HOGENOM; HOG000268119; -.
DR   KO; K01929; -.
DR   OMA; SYNNHWG; -.
DR   OrthoDB; 1861122at2; -.
DR   BioCyc; MSP313603:G1GNS-253-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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   HAMAP; MF_02019; MurF; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR035911; MurE/MurF_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; A4ATW2.
DR   SWISS-2DPAGE; A4ATW2.
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:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:EAR00882.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   DOMAIN       16     84       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN       96    275       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      299    377       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND      97    103       ATP. {ECO:0000256|HAMAP-Rule:MF_02019}.
SQ   SEQUENCE   425 AA;  47548 MW;  761A62AA960436E6 CRC64;
     MNIEQLHQIF LQFPLVCTDT RKIKINCLFF ALKGDNFNGN EYADEALKKG ASYSIVDEEK
     YATSDKTILV KDVLQTLQKL ATFHRNFYSA KVIGLTGSNG KTTTKELVNA VLSSKYKTIA
     TIGNLNNHIG VPLTLLTIKE DTEIAIVEMG ANHQKEIEFL CSLAQPDYGY ITNFGKAHLE
     GFGSVEGVIE GKSELYDYLL ANQKSIFLNA DDPIQHKKLG HYIKKYGFTT AKKEYFKIKF
     LISDPYVSLS VEDIEINSKL IGNYNFTNCC AAVLMGKYFN VELNDIKTAI ESYIPQNNRS
     QIIESNGTRI ILDAYNANPT SMKVALENFN SLSGEPKIAF LGDMFELGAT SNEEHQNIAD
     LTSSLDISEV FLVGDNFYRT KTPLKKFKNY EALALYLADV ELPSNSTILI KGSRGMALER
     LLELL
//

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