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ALX_ECO57
ID   ALX_ECO57               Reviewed;         321 AA.
AC   Q8XAJ0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative membrane-bound redox modulator Alx;
GN   Name=alx; OrderedLocusNames=Z4441, ECs3970;
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).
CC   -!- FUNCTION: Has been proposed to be a redox modulator.
CC       {ECO:0000250|UniProtKB:P42601}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P42601}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TerC family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58221.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37393.1; -; Genomic_DNA.
DR   PIR; A85970; A85970.
DR   PIR; B91125; B91125.
DR   RefSeq; NP_311997.1; NC_002695.1.
DR   RefSeq; WP_001098809.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XAJ0; -.
DR   STRING; 155864.EDL933_4310; -.
DR   EnsemblBacteria; AAG58221; AAG58221; Z4441.
DR   EnsemblBacteria; BAB37393; BAB37393; ECs_3970.
DR   GeneID; 916186; -.
DR   KEGG; ece:Z4441; -.
DR   KEGG; ecs:ECs_3970; -.
DR   PATRIC; fig|386585.9.peg.4144; -.
DR   eggNOG; COG0861; Bacteria.
DR   HOGENOM; CLU_045644_1_2_6; -.
DR   OMA; ADHAREY; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR005496; Integral_membrane_TerC.
DR   InterPro; IPR022369; Integral_membrane_TerC_rswitch.
DR   PANTHER; PTHR30238:SF0; PTHR30238:SF0; 1.
DR   Pfam; PF03741; TerC; 1.
DR   TIGRFAMs; TIGR03718; R_switched_Alx; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..321
FT                   /note="Putative membrane-bound redox modulator Alx"
FT                   /id="PRO_0000103412"
FT   TOPO_DOM        1..6
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..89
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..225
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..286
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..321
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  35951 MW;  B6FB7173442799C3 CRC64;
     MNTVGTPLLW GGFAVVVAIM LAIDLLLQGR RGAHAMTMKQ AAAWSLVWVT LSLLFNAAFW
     WYLVQTEGRA VADPQALAFL TGYLIEKSLA VDNVFVWLML FSYFSVPAAL QRRVLVYGVL
     GAIVLRTIMI FTGSWLISQF DWILYIFGAF LLFTGVKMAL AHEDESGIGD KPLVRWLRGH
     LRMTDTIDNE HFFVRKNGLL YATPLMLVLI LVELSDVIFA VDSIPAIFAV TTDPFIVLTS
     NLFAILGLRA MYFLLAGVAE RFSMLKYGLA VILVFIGIKM LIVDFYHIPI AVSLGVVFGI
     LVMTFIINAW VNYRHDKQRV G
 
 
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