ID Q0AZZ9_SYNWW Unreviewed; 548 AA. AC Q0AZZ9; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 76. DE SubName: Full=Putative methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:ABI67705.1}; GN OrderedLocusNames=Swol_0365 {ECO:0000313|EMBL:ABI67705.1}; OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae; OC Syntrophomonas. OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI67705.1, ECO:0000313|Proteomes:UP000001968}; RN [1] {ECO:0000313|Proteomes:UP000001968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968}; RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x; RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.; RT "The genome of Syntrophomonas wolfei: new insights into syntrophic RT metabolism and biohydrogen production."; RL Environ. Microbiol. 12:2289-2301(2010). 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; CP000448; ABI67705.1; -; Genomic_DNA. DR RefSeq; WP_011639813.1; NC_008346.1. DR AlphaFoldDB; Q0AZZ9; -. DR STRING; 335541.Swol_0365; -. DR KEGG; swo:Swol_0365; -. DR eggNOG; COG0840; Bacteria. DR HOGENOM; CLU_000445_107_27_9; -. DR Proteomes; UP000001968; 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; cd06225; HAMP; 1. 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; IPR024478; HlyB_4HB_MCP. DR InterPro; IPR004089; MCPsignal_dom. DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1. DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1. DR Pfam; PF12729; 4HB_MCP_1; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM00304; HAMP; 1. 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:UP000001968}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE- KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6..30 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 208..228 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 233..285 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 283..519 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000259|PROSITE:PS50111" SQ SEQUENCE 548 AA; 59461 MW; A22EAB3F3595CE26 CRC64; MLNRLNIAVQ VIAVFIIISI FSIVVGIVGV KANDKALKHL IKIEDVNFPS AEELAKIALS QSMVLTAERG LINNDMLESK LHQSQYDRIE LEKQIAQEAI KNYLTLPQAS EEKQMWEQFL PLWETWLSHS QQVVQIAREK DALLSELGNL DAPQIKEINT TLLNASLQSR ESFLKAQDSL NTLIDINTQA AHNEGVIAKQ EVTLSFRLML GGMFLSILLA LILGYYLLRT LRQRLVNPVK DMGEIAHQAA SGDLSVDIAI GSNDEIGQLA KALKNMILQI RGIISEVSEK SNYLSSSAGQ LNANYQQSTV QANQTATTMG EIASAVSQVA TSVQEISQVS VKTSDFANNG KEGVAIIGSQ MQAITDSTTH ASDVIHSLSQ KAKEITQIVE LISSISDQTN LLALNAAIEA ARAGEQGRGF AVVAEEVRKL AEQSAQAAKR IKDLIISIQL ESQKAEEAMA FGSQEVEAGN RVVNELKESF NAIIEAVHIL SDQIQEAASA TEETSAGVQE VAATVEEQTA SMGDVASAAE SLAMLAKELS ELVKRFKL //