ID A0A1K1N289_9GAMM Unreviewed; 567 AA.
AC A0A1K1N289;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SFW29447.1};
GN ORFNames=SAMN02800691_0832 {ECO:0000313|EMBL:SFW29447.1};
OS Luteibacter sp. UNCMF366Tsu5.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1502758 {ECO:0000313|EMBL:SFW29447.1, ECO:0000313|Proteomes:UP000182005};
RN [1] {ECO:0000313|EMBL:SFW29447.1, ECO:0000313|Proteomes:UP000182005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCMF366Tsu5.1 {ECO:0000313|EMBL:SFW29447.1,
RC ECO:0000313|Proteomes:UP000182005};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FPIS01000001; SFW29447.1; -; Genomic_DNA.
DR RefSeq; WP_072321227.1; NZ_FPIS01000001.1.
DR AlphaFoldDB; A0A1K1N289; -.
DR STRING; 1502758.SAMN02800691_0832; -.
DR OrthoDB; 8744489at2; -.
DR Proteomes; UP000182005; 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 CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF05227; CHASE3; 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:UP000182005};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..268
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 273..502
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 285..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..511
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 288..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 59245 MW; CAE7F4BE07FAF2B7 CRC64;
MQFIKLASRN KLIFSGFAAI AMVVIVLVGL VYAALQTMER STRMDLHSNE VLRVEGALLG
ALVNIETGER GYLITGKEAS LAPMIAGQAA YADALSKLRQ LTIDNAEQQK RLADIDAVYR
SWTTDAIDPV IALQKKQPEN SGSSAEALAY EREGKGKARM DEMRDLLGKF VGAETALLDE
RSAQAATTRA RTDGILLGGG LLALLAIVGV ATALVRSILA PLEHASAVTA RIAAGHLGES
VSVTRNDDLG RMLNALHAMD ENLARIVGAV RENAVQVEHA ARDISAGNDD LSNRTQEQAS
SLEETAASME EMSSAVKQNA SGAALAQQIS QGLRTDAKNG GAVADEAVEA MKQISEASRN
IGEIAVLIDE IAFQTNLLAL NAAVEAARAG EQGRGFAVVA AEVRNLAQRS AAAAKDIKSL
IGTTVQRVST GSDLVNRTGQ ALVTIGNSAT KVADIVSEIS AASQEQSAGV EQVNVAVASL
DDVTQQNAAL VEEASAASRQ ALELAQELTR QVAFFKLADS AAVVAGASSK PSPQPVKAAP
VSAPREPLMA MAPAAQPALA SGQWREF
//
