ID Q2RWQ9_RHORT Unreviewed; 736 AA. AC Q2RWQ9; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 115. DE SubName: Full=Chemotaxis sensory transducer {ECO:0000313|EMBL:ABC21436.1}; GN OrderedLocusNames=Rru_A0632 {ECO:0000313|EMBL:ABC21436.1}; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / OS NCIMB 8255 / S1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC21436.1, ECO:0000313|Proteomes:UP000001929}; RN [1] {ECO:0000313|EMBL:ABC21436.1, ECO:0000313|Proteomes:UP000001929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1 RC {ECO:0000313|Proteomes:UP000001929}; RX PubMed=21886856; DOI=10.4056/sigs.1804360; RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K., RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C., RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y., RA Roberts G.P., Reslewic S., Schwartz D.C.; RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1)."; RL Stand. Genomic Sci. 4:293-302(2011). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the hemerythrin family. CC {ECO:0000256|ARBA:ARBA00010587}. 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; CP000230; ABC21436.1; -; Genomic_DNA. DR RefSeq; YP_425723.1; NC_007643.1. DR AlphaFoldDB; Q2RWQ9; -. DR STRING; 269796.Rru_A0632; -. DR EnsemblBacteria; ABC21436; ABC21436; Rru_A0632. DR KEGG; rru:Rru_A0632; -. DR PATRIC; fig|269796.9.peg.688; -. DR eggNOG; COG0840; Bacteria. DR eggNOG; COG4564; Bacteria. DR HOGENOM; CLU_000445_107_21_5; -. DR PhylomeDB; Q2RWQ9; -. DR Proteomes; UP000001929; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; 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; cd12107; Hemerythrin; 1. DR CDD; cd11386; MCP_signal; 1. DR CDD; cd18774; PDC2_HK_sensor; 1. DR Gene3D; 6.10.340.10; -; 1. DR Gene3D; 1.20.120.50; Hemerythrin-like; 1. DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt. DR InterPro; IPR016131; Haemerythrin_Fe_BS. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR012312; Hemerythrin-like. DR InterPro; IPR035938; Hemerythrin-like_sf. DR InterPro; IPR012827; Hemerythrin_metal-bd. DR InterPro; IPR004089; MCPsignal_dom. DR InterPro; IPR033480; sCache_2. DR InterPro; IPR000727; T_SNARE_dom. DR NCBIfam; NF033749; bact_hemeryth; 1. DR NCBIfam; TIGR02481; hemeryth_dom; 1. DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1. DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF01814; Hemerythrin; 1. DR Pfam; PF00015; MCPsignal; 1. DR Pfam; PF17200; sCache_2; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM01049; Cache_2; 1. DR SMART; SM00304; HAMP; 1. DR SMART; SM00283; MA; 1. DR SUPFAM; SSF47188; Hemerythrin-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. DR PROSITE; PS00550; HEMERYTHRINS; 1. DR PROSITE; PS50192; T_SNARE; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Methylation {ECO:0000256|ARBA:ARBA00022481}; KW Reference proteome {ECO:0000313|Proteomes:UP000001929}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE- KW ProRule:PRU00284}; Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT DOMAIN 237..294 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 334..563 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000259|PROSITE:PS50111" FT DOMAIN 486..548 FT /note="T-SNARE coiled-coil homology" FT /evidence="ECO:0000259|PROSITE:PS50192" SQ SEQUENCE 736 AA; 79979 MW; 5616EC896E44F73F CRC64; MVCRKKPSLL RERLPYPFQV ISDKIMILDR LPVSRKLFAL VLVSLLGIGA TAILALSQVH DVMMEDRRAK VRAIVDLAFS QTADLADRAA RGAITSEAAQ AGAIEILRRA RYDGGEYLFI IDTKGRSVMH PLAPEMEGKD MSGVKDAKGT AMFAEMARLA VSQGSGFFAY EWQRGAQGTA SPKISYVRRL PQWDWVIGSG IYIDDVEAAF TRQALIFAAV VAAVVAVLLG LSLVIGRGIA GPLVAMTGRM RKMASGDLET AIPGEATADQ RRDEVGEMAG ALVVFRETLR DAKRLAEEHR HEEEQKHIRR QQVDEQIRAF EMTVVRLLDG LVSADQSVRS TTTRLVDGAR DTMSEANEVA ASAEHASANV ETVASAAEEL SASIQEIARQ VEQSSGVARR AVEETGEATK GIAELEERVG QITDIVKLIS DIASQTNLLA LNATIEAARA GDAGKGFAVV AEEVKNLANQ TQKATKDITG RIADVEEATT RSVEAIRDVS KVIGEIHEIS ASISAAVEEQ GAATREIARN VDEAATGTNR VSSAIGRVRA AAEEANSEAG DMERASRDLG HQAEVLKGEV AEFLQGIRLG DGEDHALVTW SDDLATGDAH VDEDHRKLMA LVNSVYGHVK QGEAGAALEA SFGELKRYSI EHFAEEEAFM ATVNFPQAET HRRQHQHFLG RSDALFEAYR RGADTAAVEL MGLLGSWWET HIRIYDTELA HFVRRRQATP TLRRSA //