ID A0A268E112_9BACI Unreviewed; 569 AA.
AC A0A268E112;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHH83_22065 {ECO:0000313|EMBL:PAD66812.1};
OS Bacillus sp. 7586-K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD66812.1, ECO:0000313|Proteomes:UP000216230};
RN [1] {ECO:0000313|EMBL:PAD66812.1, ECO:0000313|Proteomes:UP000216230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7586-K {ECO:0000313|EMBL:PAD66812.1,
RC ECO:0000313|Proteomes:UP000216230};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) 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:PAD66812.1}.
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DR EMBL; NPCL01000119; PAD66812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268E112; -.
DR OrthoDB; 358716at2; -.
DR Proteomes; UP000216230; 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; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000216230};
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 9..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..263
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 282..518
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 569 AA; 62261 MW; B1C71BE580B0E63A CRC64;
MKWLKDLKII FKITIIAVIS LIGIVIVGLT GFSEIRNMGN KLDDMYTDNL KPIETVSKIK
SNLQYTQQNL IELMVNTDES RNEELLAELT AKLEENEKLL ETYHTNDQDQ LEKLDRVTNL
SNQITDSVAK VIDLASANKN NEAYELYVAE TDPILQLIDE TYTDLIELNS NFAKAVNNQN
SKDIQYATII MISITIGCII LFGLVSLIIA GLIYKPVKQM EGLMKRAENG DLSVQSDYQS
KDEIGSLSTS FNNMLIQLNQ LISKIGLSSD HVAAASEQLM TSAEETNRAS EHIAEASTVL
ASSAETSVRE TEQASTSIQE MAMGINHITE SISLVSEHSN TTTAESEKGN VFLKKTINQM
DSINQTVLES SSIIKDLGQR SKEIENIVAM ISTISNQTNL LALNAAIEAA RAGEHGKGFA
VVADEVRKLA EESNRSAEQI TQLIQEIQNN TLNAVEAMDK CMTEMKAGLD LINQTGESFN
QILHSATDVS KQSEEVTAAA QQMSASVEQT AYGILEISKN AETSASSSQT VAAGAEEQLA
SMEEITASAQ TLAKMAEELQ TMVSTFKLK
//