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WZZE_ECO57
ID   WZZE_ECO57              Reviewed;         348 AA.
AC   P0AG01; P25905; P76752;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=ECA polysaccharide chain length modulation protein {ECO:0000255|HAMAP-Rule:MF_02025};
GN   Name=wzzE {ECO:0000255|HAMAP-Rule:MF_02025}; Synonyms=wzz;
GN   OrderedLocusNames=Z5296, ECs4718;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 54-318, AND SUBUNIT.
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=18204465; DOI=10.1038/nsmb.1374;
RA   Tocilj A., Munger C., Proteau A., Morona R., Purins L., Ajamian E.,
RA   Wagner J., Papadopoulos M., Van Den Bosch L., Rubinstein J.L., Fethiere J.,
RA   Matte A., Cygler M.;
RT   "Bacterial polysaccharide co-polymerases share a common framework for
RT   control of polymer length.";
RL   Nat. Struct. Mol. Biol. 15:130-138(2008).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (5.99 ANGSTROMS) OF 2-348, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=25307743; DOI=10.1002/pro.2586;
RA   Kalynych S., Cherney M., Bostina M., Rouiller I., Cygler M.;
RT   "Quaternary structure of WzzB and WzzE polysaccharide copolymerases.";
RL   Protein Sci. 24:58-69(2015).
CC   -!- FUNCTION: Modulates the polysaccharide chain length of enterobacterial
CC       common antigen (ECA). {ECO:0000255|HAMAP-Rule:MF_02025}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC       antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02025}.
CC   -!- SUBUNIT: Homooctamer (PubMed:18204465, PubMed:25307743). Probably part
CC       of a complex composed of WzxE, WzyE and WzzE (By similarity).
CC       {ECO:0000255|HAMAP-Rule:MF_02025, ECO:0000269|PubMed:18204465,
CC       ECO:0000269|PubMed:25307743}.
CC   -!- INTERACTION:
CC       P0AG01; P0AG01: wzzE; NbExp=5; IntAct=EBI-15680585, EBI-15680585;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02025, ECO:0000269|PubMed:25307743}; Multi-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_02025}.
CC   -!- SIMILARITY: Belongs to the WzzB/Cld/Rol family. {ECO:0000255|HAMAP-
CC       Rule:MF_02025}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG58980.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB38141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG58980.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB38141.1; ALT_INIT; Genomic_DNA.
DR   PIR; F91218; F91218.
DR   PIR; H86064; H86064.
DR   RefSeq; NP_312745.2; NC_002695.1.
DR   RefSeq; WP_001295256.1; NZ_SWKA01000005.1.
DR   PDB; 3B8O; X-ray; 2.40 A; A/B/C/D/E/F/G/H=54-318.
DR   PDB; 4WL1; X-ray; 5.99 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f=2-348.
DR   PDBsum; 3B8O; -.
DR   PDBsum; 4WL1; -.
DR   AlphaFoldDB; P0AG01; -.
DR   SMR; P0AG01; -.
DR   DIP; DIP-46395N; -.
DR   STRING; 155864.EDL933_5105; -.
DR   EnsemblBacteria; AAG58980; AAG58980; Z5296.
DR   EnsemblBacteria; BAB38141; BAB38141; ECs_4718.
DR   GeneID; 58459601; -.
DR   GeneID; 915243; -.
DR   KEGG; ece:Z5296; -.
DR   KEGG; ecs:ECs_4718; -.
DR   PATRIC; fig|386585.9.peg.4922; -.
DR   eggNOG; COG3765; Bacteria.
DR   HOGENOM; CLU_060925_2_1_6; -.
DR   OMA; GLCCTLW; -.
DR   UniPathway; UPA00566; -.
DR   EvolutionaryTrace; P0AG01; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_02025; WzzE; 1.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   InterPro; IPR032895; WzzE.
DR   Pfam; PF02706; Wzz; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..348
FT                   /note="ECA polysaccharide chain length modulation protein"
FT                   /id="PRO_0000065997"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02025"
FT   TOPO_DOM        52..322
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02025"
FT   TOPO_DOM        344..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           71..80
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           96..109
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           111..119
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           122..125
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           132..143
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   TURN            153..156
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   STRAND          160..167
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           168..228
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           266..274
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   HELIX           280..294
FT                   /evidence="ECO:0007829|PDB:3B8O"
FT   STRAND          306..309
FT                   /evidence="ECO:0007829|PDB:3B8O"
SQ   SEQUENCE   348 AA;  39489 MW;  4BE76BE122A1679F CRC64;
     MTQPMPGKPA EDAENELDIR GLFRTLWAGK LWIIGMGLAF ALIALAYTFF ARQEWSSTAI
     TDRPTVNMLG GYYSQQQFLR NLDVRSNMAS ADQPSVMDEA YKEFVMQLAS WDTRREFWLQ
     TDYYKQRMVG NSKADAALLD EMINNIQFIP GDFTRAVNDS VKLIAETAPD ANNLLRQYVA
     FASQRAASHL NDELKGAWAA RTIQMKAQVK RQEEVAKAIY DRRMNSIEQA LKIAEQHNIS
     RSATDVPAEE LPDSEMFLLG RPMLQARLEN LQAVGPAFDL DYDQNRAMLN TLNVGPTLDP
     RFQTYRYLRT PEEPVKRDSP RRAFLMIMWG IVGGLIGAGV ALTRRCSK
 
 
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