ID G2FJC8_9GAMM Unreviewed; 623 AA.
AC G2FJC8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Protein PilJ {ECO:0000313|EMBL:EGW53075.1};
GN Name=pilJ {ECO:0000313|EMBL:EGW53075.1};
GN ORFNames=TevJSym_bn00010 {ECO:0000313|EMBL:EGW53075.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53075.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW53075.1, 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 -!- 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:EGW53075.1}.
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DR EMBL; AFZB01000040; EGW53075.1; -; Genomic_DNA.
DR AlphaFoldDB; G2FJC8; -.
DR PATRIC; fig|1049564.3.peg.3008; -.
DR eggNOG; COG0840; Bacteria.
DR Proteomes; UP000005167; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
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; 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; 2.
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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
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 259..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 294..345
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 350..586
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 623 AA; 66383 MW; BEF8334C1BB6F5D0 CRC64;
MLAQRIAKFA ISAARGDRQA FAPLRSARDQ FETVMTELKN GSEADDLPGS PVQVMLPLRK
VENAWLELRQ NADEILAAQE PILAIGEFIG VISEFVPQLQ ELSEEVAQVL IEKNASPQQI
FIASEQRMLA ERIQAKVSLV LAGGQQTAAA IDQFTRDADR FGRVLDGLLE GDPDLGVTKV
ADPVAEQRLR DIATLFGTVS DHADEIIENI PAVLPALEAA SSMNEISDRT SEATENLIKV
YGESPGRIEI LGVKAGPGMV AAFGGLAAAF LIILGFRLVL DARRREEASK EQNESNQRAI
LRLLDEMGDL ADGDLTVTAS VTEDITGAIA DSINYAIEAL RELVTTINQT AEQVSSSTQE
TRATAMHLAE ASVHQAEQIT DANDAIKSMS LAIDQMSNDA AESAEVALRS VDIASNGAET
VRNTIQGMDA IREQIQETSK RIKRLGESSQ EIGDIVELID DIADQTNILA LNAAMQAAMA
GEAGRGFAVV ADEVQRLAER SINATKQIEA LVKTIQADTN EAVTSMEAST SGVVRGAKLA
EDAGEALMEI ESVSQYISDL TGKIAESAKA QSEAAVGVNA TMNVIQEITT QTSDGTSQTA
ASIGALADLS DELQKSVAGF RLP
//