ID H9UDF5_FERPD Unreviewed; 674 AA.
AC H9UDF5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AFG35548.1};
GN OrderedLocusNames=Ferpe_1479 {ECO:0000313|EMBL:AFG35548.1};
OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG35548.1, ECO:0000313|Proteomes:UP000007384};
RN [1] {ECO:0000313|Proteomes:UP000007384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL Submitted (MAR-2012) 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; CP003260; AFG35548.1; -; Genomic_DNA.
DR RefSeq; WP_014451985.1; NC_017095.1.
DR AlphaFoldDB; H9UDF5; -.
DR STRING; 771875.Ferpe_1479; -.
DR KEGG; fpe:Ferpe_1479; -.
DR PATRIC; fig|771875.3.peg.1485; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_415562_0_0_0; -.
DR OrthoDB; 39115at2; -.
DR Proteomes; UP000007384; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
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 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 398..634
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 674 AA; 76613 MW; 181CAA950368FDDB CRC64;
MKTFLTKNIL IALLGLLTIS LIVAFMGAYR NVPGIEEFND AKVIVNGEEK PFPYFVADKE
NNHYTMQIKI DGAKYKGKTL AFSVTANQYV KVYQNGMLIY SISSDKGSVN PWHRYFALPL
QGDVIIELSF ISNGGIERKF YIGEHDDIIK FIERANLIEE SMFYLGSGFM IGLFIIVLLL
ALALKEKTFL YGAIVVISPL LTSIDEMNLF LHPFILWKKL AILGAALSMY FAYLFTNEIF
KRRPTKLEKV YILLYWLLFL PVILARSMTQ LKNSYAIFYL YSLILLLSVL VILVKRVKTK
QEQLILFGFS AVIGATFLSL LSVANIVKIE FMFFNIGQVF FGLTIAIYVS ARTIEVFRNT
QSMNEAISKL MDEQTNYIQN LVASRDKVNE LSASSVKYFE EIEALYKNLS SSVQNAGNTL
EKLQNTVEYF ESFLDEMVKT SSLLEETVGK SDKVMSDIIS ISESSKENFS EIENIVTNFN
QMSNKLKSTF DELYNDFAKI KDISNLIKSI AVQTNLLSLN ASIEAARAGE AGKSFAVVAN
EIRKLANEAS EFAERIENNI TSISNRFEGF SAELLNLFKN VEIISESNRK FSEAIYRFFD
SVQLLTQDFE KVEETFEKQS SEISNLKDSI YEITKISEEL KQALDLFGET QKKIEETFSI
IMNQIVEVQN ALKI
//
