ID G2FBQ5_9GAMM Unreviewed; 685 AA.
AC G2FBQ5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:EGW55736.1};
GN ORFNames=TevJSym_ab00880 {ECO:0000313|EMBL:EGW55736.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW55736.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW55736.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW55736.1}.
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DR EMBL; AFZB01000002; EGW55736.1; -; Genomic_DNA.
DR RefSeq; WP_006473750.1; NZ_AFZB01000002.1.
DR AlphaFoldDB; G2FBQ5; -.
DR eggNOG; COG0840; Bacteria.
DR Proteomes; UP000005167; Unassembled WGS sequence.
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 CDD; cd06225; HAMP; 1.
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 PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..408
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 413..649
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 163..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 73756 MW; 920F7D3A03EA3791 CRC64;
MRQVGIGAKI GGGFLVAGLI LAASGLVGYW VISNLSSALA EITGPVWSSM ESANGAIRGV
QKQLIAVDQI LAGRDSAQRT EMAEAERLTL EAIVRLKTSG RIAPQQLQAL DGEIEVFVQA
REELIRIHNA FQSAEAALSA NAAAFQRLLV DVERLASQQM LERDLNSRSE EELGEFEEGD
DRAPDEGEGD PRAVVSAAGE ARLAVLSQLD LYRRFKQNSP PQDLDRQLGV IGEDLLYALE
QISEDQLFSQ PIRSGENVGK SHSQLLMEQL QEHRELLSAS IERYAVRRQA HRDYTQVAEH
LMQTVEQMTA DNRAQVEVET GELQRLVSTG ANSIIIAILL GLLVAVLAFM LTLRAIVRPI
REVRDQLGSL SQGEGGLNVT LSVKGSDETA QLAQGFNAFT SKLRDMIAGV QESMNRLVST
TDDISRIADK AGEAVRYQQQ EVASVTNAVA ELTGSLQEVT ANTFQAAERA GLADKETSQG
RALVQQTLLL IQVVATEVEQ ATRVVNELGE KSESIGGVLD VIRGISEQTN LLALNAAIEA
ARAGEQGRGF AVVADEVRGL AARTNDSISE IQVMIDQLQQ GTSQAIKVMT QARSQTQACV
EPANQADTRL DQIAGMVRSI TELNRGIANA AEAQHLTVVG VEKNLAGINE VAANTSSSAV
ELTTSTQVLS QLADELQALV GEFRV
//