(data stored in SCRATCH zone)

SWISSPROT: A8FQ95_SHESH

ID   A8FQ95_SHESH            Unreviewed;       493 AA.
AC   A8FQ95;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 83.
DE   RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00766893};
DE            EC=6.3.2.- {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00382149};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
GN   OrderedLocusNames=Ssed_0405 {ECO:0000313|EMBL:ABV35018.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35018.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35018.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35018.1,
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: Catalyzes the addition of an amino acid to the
CC       nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
CC       (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135,
CC       ECO:0000256|SAAS:SAAS00382078}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00382122}.
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
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DR   EMBL; CP000821; ABV35018.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8FQ95; -.
DR   STRING; 425104.Ssed_0405; -.
DR   EnsemblBacteria; ABV35018; ABV35018; Ssed_0405.
DR   KEGG; sse:Ssed_0405; -.
DR   eggNOG; ENOG4107EEN; Bacteria.
DR   eggNOG; COG0769; LUCA.
DR   HOGENOM; HOG000268118; -.
DR   KO; K01928; -.
DR   OMA; CFMEVSS; -.
DR   OrthoDB; POG091H0082; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; 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_00208; MurE; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
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; TIGR01085; murE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQ95.
DR   SWISS-2DPAGE; A8FQ95.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00085443};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00085467};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00085386};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00085370};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00085405};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00085419};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00459363};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00085432};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00085400}.
FT   DOMAIN       22     98       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      110    316       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      337    422       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     112    118       ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION       41     43       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      154    155       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING      24     24       UDP-MurNAc-L-Ala-D-Glu; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00208}.
FT   BINDING      26     26       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     153    153       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     181    181       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     187    187       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     189    189       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   MOD_RES     221    221       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
SQ   SEQUENCE   493 AA;  53386 MW;  EFCA1AEE0B9A1C8B CRC64;
     MLLRDLLAPW FHYAGSESFN KLTLDSRAVG PGDLFIAIPG HQADGRKYIR SAVQQGAVAS
     LVHTDDPESH GKCVDDEGKQ ILFFQLNRQL SALAAQAYPL SAERLKLVGV TGTNGKTSIT
     QLMAQLVTLL GKQSAVMGTL GNGLWGDLVD SGNTTADAIT MMAQLQEFDA QGAELCAMEV
     SSHGLIQGRV EAVPFDVAVF TNLSRDHLDY HGTMQAYGDA KKRLFNFPSL SSGLINLDDE
     IGKQWLAEHD TGKYTSFSIH GEPASIENSK AIYTQNNHFH HQGVDAKLVW PGGHADLCSP
     LLGSFNLSNL IAALGALYLL GFDMHSLVAV VPKLQAVAGR MERFTTPDDV TIVVDYAHTP
     DAIEQALKAL RGHCDGELWC LFGCGGDRDK GKRPLMAQAA EKYADRVVVT SDNARSEQPD
     VIINDILEGL TAPDKALTQV DREVAIRQVV ANAKAGDLVL LAGKGHETYQ EIAGVRRQYD
     ERALARELSE AQV
//

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