ID A0A1F8MT71_9CHLR Unreviewed; 680 AA.
AC A0A1F8MT71;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Y72_01325 {ECO:0000313|EMBL:OGO01818.1};
OS Chloroflexi bacterium RBG_13_53_26.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797629 {ECO:0000313|EMBL:OGO01818.1, ECO:0000313|Proteomes:UP000180304};
RN [1] {ECO:0000313|EMBL:OGO01818.1, ECO:0000313|Proteomes:UP000180304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGO01818.1}.
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DR EMBL; MGMW01000091; OGO01818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MT71; -.
DR Proteomes; UP000180304; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 3.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF17200; sCache_2; 1.
DR SMART; SM01049; Cache_2; 1.
DR SMART; SM00304; HAMP; 2.
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; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 201..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 223..275
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 361..597
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 621..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 73744 MW; 60F476C104B1455F CRC64;
MARLGLLKRI RLGIMWKMSL AALLVVSILV VYMSVYVFPE MKRDLFHEKE IKTQEEVQVA
WGMLDYCYGL ESSGLVTRAE AQRYALAAIG GLRYGEDDEG YFWINDYRPV LLVDPFRSDI
VNTDVSNFID AEGNAIFVDI VDICSTQGEG FYSYMWQYKD QSGRVVPKLA YVKSFDPWGW
IVGTGIYTED VMAPINSQRT LMAWIGGATA VLCLFVFWLI TRLAIAKPLK SLVRTSQALA
EGDVEQEISV KSRDEVGDLA EAYRRVVDYM KEMAGVTKRI AAGDLTMEIE PKSEKDVLSN
AFSQMVASQR DLIGKVKATA ASVSEAGRQL SRASEQTAQA TQQIASTIQM IAKGAGEQSV
TLQESTNNMG QLSVTIEQIS RGAQEQSRGV EEATDMVSQV STAAGQVSAN ARAGSEAWKG
TASSAEKGAL KTHETIEGME KIKRAMDVVS MKVADLGHRS DEIGKIVATI DDIAAQTNLL
ALNAAIEAAR AGEQGRGFAV VADEVRKLAE RSSTATKEIA VLIGGIQGGV REAVSAMQQG
GREVEGGYKL AADAGEALDD ILERARDVGR QVEQISRAAQ ELDALSDDMV KVIDRINKIV
EQNVVATEQM SESALNMSRS VETTSAVAEE NSAAAQEVSA SAEEMSAQVE EVLASAQSLA
DMSEELEKSV MVFRTEVSGD
//