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Database: UniProt
Entry: A0A1S9IHX5_9CLOT
LinkDB: A0A1S9IHX5_9CLOT
Original site: A0A1S9IHX5_9CLOT 
ID   A0A1S9IHX5_9CLOT        Unreviewed;       670 AA.
AC   A0A1S9IHX5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:OOO69919.1};
GN   ORFNames=BS638_00615 {ECO:0000313|EMBL:OOO69919.1};
OS   Clostridium tepidum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1962263 {ECO:0000313|EMBL:OOO69919.1, ECO:0000313|Proteomes:UP000190256};
RN   [1] {ECO:0000313|EMBL:OOO69919.1, ECO:0000313|Proteomes:UP000190256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IEH 97212 {ECO:0000313|EMBL:OOO69919.1,
RC   ECO:0000313|Proteomes:UP000190256};
RA   Dobritsa A.P., Kutumbaka K.K., Werner K., Wiedmann M., Asmus A.,
RA   Samadpour M.;
RT   "Clostridium tepidum sp. nov., a close relative of Clostridium sporogenes
RT   and Clostridium botulinum Group I.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OOO69919.1}.
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DR   EMBL; MRAE01000001; OOO69919.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9IHX5; -.
DR   STRING; 1962263.BS637_08025; -.
DR   OrthoDB; 9814363at2; -.
DR   Proteomes; UP000190256; 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; cd12914; PDC1_DGC_like; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF02743; dCache_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   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   Coiled coil {ECO:0000256|SAM:Coils};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          307..365
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          384..641
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          591..618
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   670 AA;  74346 MW;  388F97D0594F92B9 CRC64;
     MKSLRTKIIT MFTTIIFVLT VVLGFIVING VTKNLTQDYY SDLKTISIEK ANYIKAKIDS
     EISYMEAMAQ QDRIINKDIS WENNVYYFEK EAKRAGYVYY AFADKNGNSI LFNKKRDTVN
     IRGREYYKKA IEGKSTISDV IISAVTKKPI IIVASPIIKD GQVQGIFYGA KEATFLSDIV
     SKIKYGKTGF GIIINDKGTT VGHANKKLVL SQSNTVEIAK KDESFKSLAS LIENIISEKK
     VGNGEYEYKG TKNIVGFSPI EGTNWTIVFG GELSEILAEV HSIRNIIIIV SLIIIAIGAL
     ITYFISGKIA SPIIAVTKRM NELANLDFTI YGNEDAIKYL NREDEIGSMT RALRKMRDNI
     AEFIAKTNEA SQQIVETAEE LTAISNQSAT ASEEVAKTIE DIAKGAGNQA EDTQTSALSV
     EEMGILLEQN KEYVKDLNDA AKDIEDRKEE GFCILKELIE RTKENNKAAS SVYQIIVSNN
     ESAEKIDKAS SMIESIADQT NLLALNAAIE AARAGEQGKG FAVVAEEIRK LAEQSTNFTK
     EIKKIIDELK IKSQNAVDKM DEVKKVNQYQ SESVNDTEEK FKRIAHSINI TNNVIEKLNQ
     SEKKINENKE KIMSIMQNLS AIAQQNAAST EEASASIQQQ AASVEEIANS SQGLAQIAEE
     LDILIKKFKL
//
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