ID A0A1I6HG05_9EURY Unreviewed; 766 AA.
AC A0A1I6HG05;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SFR53274.1};
GN ORFNames=SAMN04487947_2014 {ECO:0000313|EMBL:SFR53274.1};
OS Halogeometricum rufum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=553469 {ECO:0000313|EMBL:SFR53274.1, ECO:0000313|Proteomes:UP000198531};
RN [1] {ECO:0000313|EMBL:SFR53274.1, ECO:0000313|Proteomes:UP000198531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7736 {ECO:0000313|EMBL:SFR53274.1,
RC ECO:0000313|Proteomes:UP000198531};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOYT01000002; SFR53274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6HG05; -.
DR STRING; 553469.SAMN04487947_2014; -.
DR OrthoDB; 8523at2157; -.
DR Proteomes; UP000198531; 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; 2.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 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; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 2.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 3.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
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 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 314..366
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 369..415
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 434..670
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 744..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 80338 MW; C840F698CE78AE34 CRC64;
MKVARRLDEL LPESLRRNYL AKLALLFAVV TVGVVAIGGY TYVTVAEEVS DSAERDLQTT
ANLQSEQLSG WVTSQQQTAR MVSRYNVFQT AEDSVVSQYL RREKAVLPTA VTEVHYVDTE
NRNIVASSNS DAVGTDPLPE GTAFVEGSME MPVADQVSYT RPYHRDNKTF MAFVSPVQLK
SDRVVMVVAD LSYVELTLDT ATEGSFAQVV TADGRVQFDA SGRGNYGDYG VANATAVTDG
AAGNPGVYED GANALMDERH LVAYAPVAGT DFVTVVHAPA SAVYSVENSV AGKLVALLAA
VVVGFVVLGG LIHGTTVSPL SRLANRVERL REGDLNVSLP GGRVDEFGSV VDGVAALRDD
LKAQRADARR YSDVMSEAAD GDLTVRMDRD SDSADMRTIA DAFNEMVDEL ETTVVALTAF
GETVADRSSG VAAGASEVSA ASDEIARSVE QISAGAREQA DHLADLSEEM GDLSASVEEV
SATADDLATG SAEVADRADE GREAANDALT GVEAIESETH EAVASVEELD EEIARISNVT
GVIADLAEQT NILALNASIE ASRAGEAGEG FAVVAEEVKH LAEETATYAE TIEDHVTTLQ
DKRAEVVEGI EEMREQVEAG ATQVDEALSS FDEIADEVSQ NSASVEEVAA ATGQQAGTAE
DVLSMADELA GIGEETTSEA ENVSAAAEEQ TATLDEVSDG ATRLADQASD LSELLDEFDV
SADGVDFEST LSLDGETAAR LADVVADGAS DAGGESAPTP AASDDD
//