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Database: UniProt
Entry: B1HNS2_LYSSC
LinkDB: B1HNS2_LYSSC
Original site: B1HNS2_LYSSC 
ID   B1HNS2_LYSSC            Unreviewed;       649 AA.
AC   B1HNS2;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ACA42135.1};
GN   OrderedLocusNames=Bsph_4691 {ECO:0000313|EMBL:ACA42135.1};
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA42135.1, ECO:0000313|Proteomes:UP000002164};
RN   [1] {ECO:0000313|EMBL:ACA42135.1, ECO:0000313|Proteomes:UP000002164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41 {ECO:0000313|EMBL:ACA42135.1,
RC   ECO:0000313|Proteomes:UP000002164};
RX   PubMed=18296527; DOI=10.1128/JB.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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}.
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DR   EMBL; CP000817; ACA42135.1; -; Genomic_DNA.
DR   RefSeq; WP_012296136.1; NC_010382.1.
DR   AlphaFoldDB; B1HNS2; -.
DR   EnsemblBacteria; ACA42135; ACA42135; Bsph_4691.
DR   KEGG; lsp:Bsph_4691; -.
DR   HOGENOM; CLU_000445_107_19_9; -.
DR   Proteomes; UP000002164; Chromosome.
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:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd18773; PDC1_HK_sensor; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF114; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF02743; dCache_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   SUPFAM; SSF103190; Sensory domain-like; 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   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
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        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          292..344
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          363..599
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   649 AA;  70897 MW;  0C0E753AB6CF99AB CRC64;
     MKQLSVRKKL IFSFLAMLLI PTLLIGIVSY QSAEKQISEE QQASAAESVR ILNTNITNTI
     EPKLKDVQYF SKKFNESYLQ ENKIPELKSL LQEYVNMHPE VELIYLGTAD GRLLDEPAQV
     YAEDFDPRTR PWYKQALENN GQVSITAPYV TKSTDDIVIT ITQALPDGSG VIGIDLNIST
     ISDITNEIRI GETGYASLLD NNKIYIAQPE KESGTEATEN YIAKVYEQPS GTIIERDRHL
     QFVTNELTGW KVIGTMFTAE AAKAAASTLN INLMIIVVSI LVGVIFMLLM IKSVVNPINK
     LKHSALKISE GDLTEFIDIH SKDEIGQLGE AFISMKVSLK KLIRNVDQSS QHVQTSAQDL
     SANAEQNIAA SEQVADAVQQ MAISTEKQTT AIDQNAMSVE EIAKGVVEVA DSSMQVSDLS
     SHAIQLAEEG GQAVEQTVKQ MNSIHESVTQ SDTMIKTLYD RTKEIGSILE MISAISDQTN
     LLALNAAIEA ARAGEHGKGF AVVADEVRKL AEQSHHSAEQ ISALITTIQQ DTAKSVQTMV
     KASADVQDGL QLTEETNKKF ASIIASLRNI APKMEDISAS SQEMSAVVEE VSATAIELSD
     HAKLNAASTE EVAASTEQTL SSMQDIASAA KTLLDMADEL QGHVNRFHY
//
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