ID M1MSQ2_9CLOT Unreviewed; 573 AA.
AC M1MSQ2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGF54607.1};
GN ORFNames=Cspa_c08300 {ECO:0000313|EMBL:AGF54607.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF54607.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF54607.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP004121; AGF54607.1; -; Genomic_DNA.
DR RefSeq; WP_015390933.1; NZ_AOIF01000144.1.
DR AlphaFoldDB; M1MSQ2; -.
DR STRING; 36745.CLSAP_08700; -.
DR KEGG; csr:Cspa_c08300; -.
DR PATRIC; fig|931276.5.peg.786; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_9; -.
DR OrthoDB; 1887545at2; -.
DR Proteomes; UP000011728; Chromosome.
DR GO; GO:0016020; C: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 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; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011728};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..267
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 279..537
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 336..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..105
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 336..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 62745 MW; 5B8D20C558228101 CRC64;
MNILKNVKVR IKLIIAFLIV ALLIGIVGGV GIISLKNVGE NAKKMYSQNL QGVYMLTDMK
QNLTEIKSNL ADLINLKDEK DSDIKAKLEK SIEDNNAEND KYISQLKDLP KDNDENEIFE
QFNSQLNQYS IVRGNTIKLI DAGQYTGAAE QYKDIPKITD ELFNYLDKLI EANLKESSDA
NDNIVSIYTA ANTTMVILSV VGLILAIVIG LILSSDINKP LQRMRLLGEK LADYDLSYES
KVIRGDEFGQ TYGSLLKAQG NIKELIKTIL DNSQNLSASS EELSATVQEL SSKAVSVDEA
VNNIARNMEE ASAGAEEISA SIQEVDSSIS VLSQKAMDGS GNANSAKERA VQVKNDSQKA
LKESKEVSDE KQQRMAKVIE EGKVVDNIRV MAGTIAEISE QTNLLALNAA IEAARAGEMG
KGFAVVAEEV RTLAEESSGA VQNIQETIVK VQAAFKRSID TGSDILEFID KDVNKQFEAY
EKTGTQYYKD SEFVSNMSEE IAAMSEEVTA TVGQVSEAIQ NMAGTTQKST EHALKIKESM
NETTQGLEQV ASTVQGQAEL AQKLNEIVQK FRI
//
