ID A0A212S9E5_RHOAC Unreviewed; 568 AA.
AC A0A212S9E5;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SNB81835.1};
GN ORFNames=SAMN06265338_1172 {ECO:0000313|EMBL:SNB81835.1};
OS Rhodoblastus acidophilus (Rhodopseudomonas acidophila).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Rhodoblastus.
OX NCBI_TaxID=1074 {ECO:0000313|EMBL:SNB81835.1, ECO:0000313|Proteomes:UP000198418};
RN [1] {ECO:0000313|Proteomes:UP000198418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 137 {ECO:0000313|Proteomes:UP000198418};
RA Varghese N., Submissions S.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; FYDG01000017; SNB81835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212S9E5; -.
DR OrthoDB; 9814362at2; -.
DR Proteomes; UP000198418; Unassembled WGS sequence.
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 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; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198418};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..260
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 265..480
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 268..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 268..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 60496 MW; 6D1CAEE8DAA4E5DB CRC64;
MRLTIKLKLA MSFGIVIMFL CAIAGFGLYD LSKANHVLDK VIGFNSKRLE RSQNLQILSL
EALRAQKNLL LATSPDDAAK QVAAGDAAIK EFQSQWAELS ASAPPERKAY WASVDEAFKA
YLANDVNIRT KIKANDIAGA TELSLGGARV TSSRLRTVLS EGSKFYIEGM EKARLESSED
YAFIRMVTLS ATGAAVLIAA ALALWVSMSV CNGLGRAGAV MRSVADGDLS WRAENLPSDE
IGDMLGYVDT MVERLRDVVG GAAIASGNVS SGSQQLSSTS EQIAQGATEQ AAAAEEASSA
MEEMAANIKQ NADNAAQTEK IARQSAKDAE ASGEAVARAV AAMDTIAQKI TIVQEIARQT
DLLALNAAVE AARAGEHGKG FAVVASEVRK LAERSQAAAG EISHMSGDTV KSAKDAGDML
NRLVPDIRKT AELIAEISAA CREQDIGASQ INQAIQQLDQ VTQQNAGASE EMSATSEELA
SQAEELQCSI AFFRVDDEGD RRPSAVRPQA KRSVKTHALP KQGVRTQSHA TLAKKPTVQA
QQERARGFAL DLSMGGRDEQ DRDFRESA
//
