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ALX_ECOLI
ID   ALX_ECOLI               Reviewed;         321 AA.
AC   P42601; Q2M9B8; Q6BF48;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Putative membrane-bound redox modulator Alx;
GN   Name=alx {ECO:0000303|PubMed:2108134}; Synonyms=ygjT;
GN   OrderedLocusNames=b3088, JW5515;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   SEQUENCE REVISION TO 172-179.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   GENE NAME, AND INDUCTION.
RC   STRAIN=K12;
RX   PubMed=2108134; DOI=10.1128/jb.172.4.2184-2186.1990;
RA   Bingham R.J., Hall K.S., Slonczewski J.L.;
RT   "Alkaline induction of a novel gene locus, alx, in Escherichia coli.";
RL   J. Bacteriol. 172:2184-2186(1990).
RN   [5]
RP   POSSIBLE FUNCTION, AND INDUCTION.
RC   STRAIN=K12;
RX   PubMed=12107143; DOI=10.1128/jb.184.15.4246-4258.2002;
RA   Stancik L.M., Stancik D.M., Schmidt B., Barnhart D.M., Yoncheva Y.N.,
RA   Slonczewski J.L.;
RT   "pH-dependent expression of periplasmic proteins and amino acid catabolism
RT   in Escherichia coli.";
RL   J. Bacteriol. 184:4246-4258(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
CC   -!- FUNCTION: Has been proposed to be a redox modulator.
CC       {ECO:0000305|PubMed:12107143}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:15919996}.
CC   -!- INDUCTION: By extreme alkaline conditions.
CC       {ECO:0000269|PubMed:12107143, ECO:0000269|PubMed:2108134}.
CC   -!- SIMILARITY: Belongs to the TerC family. {ECO:0000305}.
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DR   EMBL; U18997; AAA57890.1; -; Genomic_DNA.
DR   EMBL; U00096; AAT48166.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77138.1; -; Genomic_DNA.
DR   PIR; E65097; E65097.
DR   RefSeq; WP_001098806.1; NZ_STEB01000001.1.
DR   RefSeq; YP_026201.1; NC_000913.3.
DR   AlphaFoldDB; P42601; -.
DR   BioGRID; 4262405; 14.
DR   STRING; 511145.b3088; -.
DR   TCDB; 2.A.109.1.7; the tellurium ion resistance (terc) family.
DR   PaxDb; P42601; -.
DR   PRIDE; P42601; -.
DR   EnsemblBacteria; AAT48166; AAT48166; b3088.
DR   EnsemblBacteria; BAE77138; BAE77138; BAE77138.
DR   GeneID; 947607; -.
DR   KEGG; ecj:JW5515; -.
DR   KEGG; eco:b3088; -.
DR   PATRIC; fig|1411691.4.peg.3641; -.
DR   EchoBASE; EB2589; -.
DR   eggNOG; COG0861; Bacteria.
DR   HOGENOM; CLU_045644_1_2_6; -.
DR   InParanoid; P42601; -.
DR   OMA; ADHAREY; -.
DR   PhylomeDB; P42601; -.
DR   BioCyc; EcoCyc:G7607-MON; -.
DR   PRO; PR:P42601; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0071467; P:cellular response to pH; IDA:EcoCyc.
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   1: Evidence at protein level;
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_0000103410"
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, ECO:0000269|PubMed:15919996"
FT   CONFLICT        172..179
FT                   /note="PLVRWLRG -> RWCAGYAV (in Ref. 1; AAA57890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  35909 MW;  B6E1C173442799C3 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 VNYRHDKQRG G
 
 
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