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Database: UniProt
Entry: A0A106BQC3_THIDE
LinkDB: A0A106BQC3_THIDE
Original site: A0A106BQC3_THIDE 
ID   A0A106BQC3_THIDE        Unreviewed;       707 AA.
AC   A0A106BQC3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KVW96705.1};
GN   ORFNames=ABW22_07080 {ECO:0000313|EMBL:KVW96705.1};
OS   Thiobacillus denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW96705.1, ECO:0000313|Proteomes:UP000064243};
RN   [1] {ECO:0000313|EMBL:KVW96705.1, ECO:0000313|Proteomes:UP000064243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG {ECO:0000313|EMBL:KVW96705.1,
RC   ECO:0000313|Proteomes:UP000064243};
RX   PubMed=26712544;
RA   Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA   van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT   "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT   Chemoautotroph.";
RL   Appl. Environ. Microbiol. 82:1486-1495(2015).
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:KVW96705.1}.
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DR   EMBL; LDUG01000019; KVW96705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A106BQC3; -.
DR   STRING; 1123392.GCA_000376425_02310; -.
DR   PATRIC; fig|36861.3.peg.892; -.
DR   OrthoDB; 9177152at2; -.
DR   Proteomes; UP000064243; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd11386; MCP_signal; 1.
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; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029095; NarX-like_N.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF13675; PilJ; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064243};
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        61..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        339..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          378..429
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          434..670
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          505..532
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   707 AA;  74291 MW;  A05ECC3270778D1E CRC64;
     MNVATTTMNG LKGLAGRMTK KVTGKSGGDH TAMIMQGVRK LADKEPGRAP LIGHLPVDRQ
     YLYAGGILVA SLILTAGFTI YSAIQLDNRT SYEARAGDLK VLSQRLPLTA QQSALGDATA
     FKKLAEGRVA FQTALTGLTE GDAEVPASSG AARTTLETIS AQWKTFDPQV ALILSQQKNL
     VTLNESVKRI NALSSDLQEV AEQLGSQLVD AGSGVREVSR ANHLVMLSQR MPKNANLLLS
     ADLIDPVVVL QLETDTTSFR DTVQVLMTGV ASRSEDSMLT MEDLGENMGE MVEAVGAVLA
     NTQPLLQSKL AANNLFVGSD KLLADASQLS QDYQSVGGAG YLLAALFGLL AIGSLVVLGL
     VNINETKSRA RKSEEENSRN QEAILRLMDE LGELAEGNLT INASVTEDIT GAVADSINYT
     VEELRSLVRG INNATLQMDQ AANQAGHISE SLQHASRRQS EGIEETSAAV VSLAQSVQQV
     SGNAAESARV AEQSLAAAEK GQQAVANAIS SMNGLREQIQ ETSKRIKRLG ESSQEIGEIV
     ELISDITEQT NVLALNAAIQ AASAGEAGRG FSVVAEEVQR LAERSADATK QIAAIVKTIQ
     SDTHDTVAAM EVSTQGVVEG AKLSDAAGQT LAEIGDVSKT LAGLIADISS ATQSQAESTA
     KVAETMQDIK AISVQTSSGT QQTAESIGSM KQLAQDLKSS VAGFKLA
//
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