ID W0DP38_9GAMM Unreviewed; 818 AA.
AC W0DP38;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:AHF00370.1};
GN ORFNames=THIAE_00190 {ECO:0000313|EMBL:AHF00370.1};
OS Thiomicrospira aerophila AL3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF00370.1, ECO:0000313|Proteomes:UP000005380};
RN [1] {ECO:0000313|EMBL:AHF00370.1, ECO:0000313|Proteomes:UP000005380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL2 {ECO:0000313|Proteomes:UP000005380};
RG DOE Joint Genome Institute;
RA Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-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; CP007030; AHF00370.1; -; Genomic_DNA.
DR RefSeq; WP_006459721.1; NZ_CP007030.1.
DR AlphaFoldDB; W0DP38; -.
DR STRING; 717772.THIAE_00190; -.
DR KEGG; tao:THIAE_00190; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_016611_0_0_6; -.
DR InParanoid; W0DP38; -.
DR OrthoDB; 6433966at2; -.
DR Proteomes; UP000005380; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.20.120.1530; -; 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; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 3.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 3.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..380
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 381..425
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 508..560
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 565..794
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 818 AA; 88977 MW; F682A53A5882F162 CRC64;
MKIKSLKHKI IFASLLVTTL VVAVVTSVMY LTQIKPLPQQ VKQQLTNDMQ VFMDSQIELK
VQSGIIGATM LSQQPILIDA LANNRQLPLR QVLANQQQHY ASVTNFRGIF SEIYDANGQS
LLRSWALDQQ PAATPPNALI TEVINTKTAQ GALGFTDRGV TITAVTPVLN SQQQLMGLVS
MLQGVGSISR DFDRIVGGNW IMLVDSEYVR ARHGHTQAID RLININPRYV VANNNWFTPE
TIQLTQSLFQ ATHGDKTNVY LNQGYLIVDL PAYDEAGQVM GRQLFIQDEQ VFTHILSAAY
QQVTVTIIGV ILGILILAGI LFGLILRLVI RPLEDLTTTM HKIDETGDFS IRVAVKSDDE
VGQTAQAINH HLVKVSDAIT QANTAIAAIA KGDLTTRIEG HYVGNLLELK TGVNASANNM
QNIIEEIARA LEQLNQGQFN FRTKVQAQGA FATILADTEN AMSQLNLTMT DIGDVVKKMA
AGQFNLSINR ELQGQLKELK DDINLSLASL NEVIKDISRV MQAQSQGDLT QSVTQECQGD
LATLKEAINQ SLAQMTEVIN EVLVSSKAVA SAAEEVSHGS ISLSDSVQQQ AASVEQTSAA
MTEIDATIKN NAEHSKTADH LQHQLETQSL QASNVMKQTI DSMAMIQQSS NQIHDIVSLI
ESIAFQTNLL ALNAAVEAAR AGEHGRGFAV VASEVRALAQ KSAEAAKEIT GLVTNSVNRI
NQGTEHATES AEIISKMHET INHVTDMLSD IANASMEQAQ GVSEINQAIG LIDNVTQQNA
ALVEETAAAA ESMKDQAQQL SQSVSFFKTH RIGTKRLN
//