ID A0A268ECZ2_9BACI Unreviewed; 675 AA.
AC A0A268ECZ2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHH83_00665 {ECO:0000313|EMBL:PAD70985.1};
OS Bacillus sp. 7586-K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD70985.1, ECO:0000313|Proteomes:UP000216230};
RN [1] {ECO:0000313|EMBL:PAD70985.1, ECO:0000313|Proteomes:UP000216230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7586-K {ECO:0000313|EMBL:PAD70985.1,
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:PAD70985.1}.
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DR EMBL; NPCL01000002; PAD70985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268ECZ2; -.
DR OrthoDB; 9760371at2; -.
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 Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
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; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..369
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 388..645
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 385..444
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 648..675
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 675 AA; 75353 MW; C64175D62A8EB4BF CRC64;
MRTRKQPKQK PAISKKRQKD RKNQFKLPQL FVGMTLKSRI ILFLLLFTLI PSLIIGNVVY
FVSSATIENK VSNMNDEIGT QVTKNVNNSL KEFENLTIVP FSNMDFMETL KDNEGLTEFQ
ILMKEREATE YFSSITFTNK FARGMLFVNE EGMLYGESDS TSKFKLENYL NSDIPEKVEE
LSGAVYWGSG VEKDFENIYL YREYDRLGTL ILMADSKLFN DVLGVEEKNI GREISVINNE
GIIIASNNQK LVGTEYKSDK KDSHLVSVSD SSNGWKVSVS TSKAYLMKEI NQVIYLVYGI
IALFVLLSVF ASILLAKGMI KPINRIVAIM KEAEKGDLTD RADYLYKNEV GQLGKSYNTM
IDNITNMIEE NKRVSTHAVK SAVDLKRIAE ESAAATEQIA SAIEEVAKGA VSQVDYSERT
NREMKELSSE INEVAHNMEK VQTITETTKK LSSQSIETIK ELTDKNEEMG TNIGQVDTTM
DALNREIAQI KDIVEMIKSV SEETNLLSLN ASIEAARAGA AGRGFAVVAS EIRKLADQTK
SSSLKIETVI ASILTQTRKS VELVKTTISL FKEQTNSIHH TMDAFENILE GTNSIISEID
YVEASIAKIN QNKEKVEIAI NEMVEVAEIS SATTEEVTAT TEEQAASAEE LGDLAASLSN
TILELEETIN KFKIK
//