ID Q5FQQ6_GLUOX Unreviewed; 491 AA. AC Q5FQQ6; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 87. DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAW61290.1}; GN OrderedLocusNames=GOX1549 {ECO:0000313|EMBL:AAW61290.1}; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61290.1, ECO:0000313|Proteomes:UP000006375}; RN [1] {ECO:0000313|EMBL:AAW61290.1, ECO:0000313|Proteomes:UP000006375} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H {ECO:0000313|EMBL:AAW61290.1, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000009; AAW61290.1; -; Genomic_DNA. DR RefSeq; WP_011253075.1; NZ_LT900338.1. DR AlphaFoldDB; Q5FQQ6; -. DR STRING; 290633.GOX1549; -. DR KEGG; gox:GOX1549; -. DR eggNOG; COG0840; Bacteria. DR HOGENOM; CLU_000445_140_0_5; -. DR Proteomes; UP000006375; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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; 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; 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 Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000006375}; KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20..36 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 56..77 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 153..201 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 206..435 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000259|PROSITE:PS50111" FT REGION 463..491 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 467..483 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 491 AA; 52597 MW; 883AA90E8AEA00A8 CRC64; MSDMRFVPMQ RSSLLRRRLL LAFAIPVAVS VCLVGWRLKT AASHTAGIWQ SVSPELALLG LFCVAGIVAF FQVAAYGDDL AGGLRQLASE GTLPRNVREA SLIRLQVLLG EARTHAERSD AMTAQAQSAL AAVRIEAEDA RQSAREEASE HERVIAVLGN AMASLRDGEL DFRLEEALPD RYDRLRQDFN DTASSLQKMM LSLNDSISTI SSGSAEIASA ADDLARRTEL QVARLEETTV SVGNVTETVR KTAAASVHAS EVASQTRDRA ERSGEVMAAA TAAMQDIQQS SIHIAQILGL IDDIAFQTNL LALNAGVEAA RAGDAGKGFA VVAAEVRALA QRSADAAKEI KGLITSSTQQ VSRGSSLVEE TGVAMKSIVE NVSEISVLIG EIATAARSQA NDLSEISVAV SQMDQNTQQN AAMVEEATAA SHNLSAEARE LVGSLQRFRL KSLHDAEKPL FESEMPASDL PSSQWGNESF QTSDEGWEEF R //