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AER_ECOLI
ID   AER_ECOLI               Reviewed;         506 AA.
AC   P50466; Q2M9D4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Aerotaxis receptor;
GN   Name=aer; Synonyms=air, yqjJ; OrderedLocusNames=b3072, JW3043;
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   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   [3]
RP   FUNCTION.
RX   PubMed=9190831; DOI=10.1128/jb.179.12.4075-4079.1997;
RA   Bibikov S.I., Biran R., Rudd K.E., Parkinson J.S.;
RT   "A signal transducer for aerotaxis in Escherichia coli.";
RL   J. Bacteriol. 179:4075-4079(1997).
RN   [4]
RP   FUNCTION.
RX   PubMed=9380671; DOI=10.1073/pnas.94.20.10541;
RA   Rebbapragada A., Johnson M.S., Harding G.P., Zuccarelli A.J.,
RA   Fletcher H.M., Zhulin I.B., Taylor B.L.;
RT   "The Aer protein and the serine chemoreceptor Tsr independently sense
RT   intracellular energy levels and transduce oxygen, redox, and energy signals
RT   for Escherichia coli behavior.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:10541-10546(1997).
RN   [5]
RP   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).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
RA   Li G., Young K.D.;
RT   "Isolation and identification of new inner membrane-associated proteins
RT   that localize to cell poles in Escherichia coli.";
RL   Mol. Microbiol. 84:276-295(2012).
CC   -!- FUNCTION: Signal transducer for aerotaxis. The aerotactic response is
CC       the accumulation of cells around air bubbles. The nature of the sensory
CC       stimulus detected by this protein is the proton motive force or
CC       cellular redox state. It uses a FAD prosthetic group as a redox sensor
CC       to monitor oxygen levels. {ECO:0000269|PubMed:9190831,
CC       ECO:0000269|PubMed:9380671}.
CC   -!- INTERACTION:
CC       P50466; P50466: aer; NbExp=4; IntAct=EBI-1130981, EBI-1130981;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:22380631}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:22380631}. Note=Predominantly localized to one cell
CC       pole in mid-to-late exponential phase, with a few smaller foci
CC       elsewhere in the cell.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; U28379; AAA89151.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76107.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77122.1; -; Genomic_DNA.
DR   PIR; E65095; E65095.
DR   RefSeq; NP_417543.1; NC_000913.3.
DR   RefSeq; WP_000094721.1; NZ_LN832404.1.
DR   AlphaFoldDB; P50466; -.
DR   SMR; P50466; -.
DR   BioGRID; 4262399; 187.
DR   DIP; DIP-9061N; -.
DR   IntAct; P50466; 4.
DR   STRING; 511145.b3072; -.
DR   PaxDb; P50466; -.
DR   PRIDE; P50466; -.
DR   EnsemblBacteria; AAC76107; AAC76107; b3072.
DR   EnsemblBacteria; BAE77122; BAE77122; BAE77122.
DR   GeneID; 945301; -.
DR   KEGG; ecj:JW3043; -.
DR   KEGG; eco:b3072; -.
DR   PATRIC; fig|1411691.4.peg.3658; -.
DR   EchoBASE; EB2789; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_26_6; -.
DR   InParanoid; P50466; -.
DR   OMA; PAMPLRW; -.
DR   PhylomeDB; P50466; -.
DR   BioCyc; EcoCyc:G7595-MON; -.
DR   PRO; PR:P50466; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:EcoCyc.
DR   GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR   GO; GO:0052131; P:positive aerotaxis; IMP:EcoCyc.
DR   GO; GO:0007165; P:signal transduction; IMP:EcoCyc.
DR   CDD; cd00130; PAS; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Chemotaxis; FAD; Flavoprotein;
KW   Membrane; Methylation; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..506
FT                   /note="Aerotaxis receptor"
FT                   /id="PRO_0000110565"
FT   TOPO_DOM        1..166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..190
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..506
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          263..492
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ   SEQUENCE   506 AA;  55066 MW;  913DEBCF14E3FD08 CRC64;
     MSSHPYVTQQ NTPLADDTTL MSTTDLQSYI THANDTFVQV SGYTLQELQG QPHNMVRHPD
     MPKAAFADMW FTLKKGEPWS GIVKNRRKNG DHYWVRANAV PMVREGKISG YMSIRTRATD
     EEIAAVEPLY KALNAGRTSK RIHKGLVVRK GWLGKLPSLP LRWRARGVMT LMFILLAAML
     WFVAAPVVTY ILCALVVLLA SACFEWQIVR PIENVAHQAL KVATGERNSV EHLNRSDELG
     LTLRAVGQLG LMCRWLINDV SSQVSSVRNG SETLAKGTDE LNEHTQQTVD NVQQTVATMN
     QMAASVKQNS ATASAADKLS ITASNAAVQG GEAMTTVIKT MDDIADSTQR IGTITSLIND
     IAFQTNILAL NAAVEAARAG EQGKGFAVVA GEVRHLASRS ANAANDIRKL IDASADKVQS
     GSQQVHAAGR TMEDIVAQVK NVTQLIAQIS HSTLEQADGL SSLTRAVDEL NLITQKNAEL
     VEESAQVSAM VKHRASRLED AVTVLH
 
 
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