ID A0A1A5XJT0_9BACL Unreviewed; 559 AA.
AC A0A1A5XJT0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A6764_11740 {ECO:0000313|EMBL:OBR53594.1};
OS Brevibacillus sp. WF146.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=319501 {ECO:0000313|EMBL:OBR53594.1};
RN [1] {ECO:0000313|EMBL:OBR53594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF146 {ECO:0000313|EMBL:OBR53594.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OBR53594.1}.
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; LXGJ01000185; OBR53594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A5XJT0; -.
DR GO; GO:0005886; C:plasma 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; 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; IPR024478; HlyB_4HB_MCP.
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; 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 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}; 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 TRANSMEM 172..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..254
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 273..509
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 559 AA; 59845 MW; 84E8C4E06FD008EB CRC64;
MKWTIGRKVT AGFLSVAFLL VMVSGLSFYF LKKVDSSYSD LMNRRAIILL NAKNIQVHAT
QLNSSLRDYL LTQNAEAMKK VEDASKQLSA LVSTSMGLAD TQETKVSLSK IEQLNKQFLK
SKDLIASAAK EQALNFATTS LFPISRDIRT IADQISERQQ QLMTQATQEN AAMVNGVVTT
VSMISVMAVI LAICIGYVVS RLIARPVVQL ASSAEKIASG DLTEDDLHVT NRDEIGELAH
SFTVMKNNLR GLIQQVRINA EQVAASAEEL TASAEQTSKA TEQIAATVQA VASGSEQQAS
SVGQSAQIVQ EMAQGIQQIA ANAQKVSASS VQAAQVAEEG NRAIQTASDQ MGSIHDKVND
LAAVIKELGE RSMEIGHIVQ VITDIASQTN LLALNAAIEA ARAGEHGRGF AVVADEVRKL
AEQSAASANQ INDVISMIRG QMEKAVASMD QVKDEVSEGM DVVTQAGTSF AHIQRSVDDV
AVQIQEVSAS TQQMSASVEE IVQSITLIRE VANETAAGTQ NVSAAAEEQL ASMEEISSSA
LALSQMSEDL QKLISRFRV
//
