ID   Q5FR96_GLUOX            Unreviewed;       445 AA.
AC   Q5FR96;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAW61100.1};
GN   OrderedLocusNames=GOX1348 {ECO:0000313|EMBL:AAW61100.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61100.1, ECO:0000313|Proteomes:UP000006375};
RN   [1] {ECO:0000313|EMBL:AAW61100.1, ECO:0000313|Proteomes:UP000006375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H {ECO:0000313|EMBL:AAW61100.1,
RC   ECO:0000313|Proteomes:UP000006375};
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000009; AAW61100.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5FR96; -.
DR   STRING; 290633.GOX1348; -.
DR   KEGG; gox:GOX1348; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_20_5; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}.
FT   DOMAIN          41..94
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          179..408
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          379..417
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   445 AA;  48803 MW;  F98E201CB4BF5E7A CRC64;
     MVEQVFQHLF VHYRHEQTLS QCAGLLFQIA LTLLIARFAI RIVAVPFEEI TAATEKVAGG
     ALNITIPCLH HQDCAGRLAR SLQSFRENSQ NQLKLQEVSA TEAREAARIQ KELSGKSESI
     RRLQSETIGT ICAGMEIVKK GDLTFTFQEH FQDRFEEFRR DFNTLIHIYR TAIARISDAT
     SMIANGTSEI ASASAELSER TERQAVNLAQ SAASLNSITQ TVGKTARSAV QARETSLETR
     AQTVVISGVM HSANTAMGEI RASSRQVESI LGLIEEIAFQ TNLLSLNAGI EAARAGEAGR
     GFDVVAKEIR ALAQRSAKSA QDIRNIITSS GRQVEEGVHF VGEADRSMKV ISQHVDGITS
     LLEEISRSTT GEAESLETIN KAINEMDQMT QRNAAMVEEV NVACRNLSNE AKDLFAELSR
     FRFAPAQPSD DWMHPANLSL AAAEI
//