ID I3TIA0_TISMK Unreviewed; 717 AA.
AC I3TIA0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:AFK52488.1};
GN OrderedLocusNames=TMO_0649 {ECO:0000313|EMBL:AFK52488.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52488.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK52488.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52488.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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}.
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DR EMBL; CP003236; AFK52488.1; -; Genomic_DNA.
DR RefSeq; WP_014744168.1; NC_017956.1.
DR AlphaFoldDB; I3TIA0; -.
DR STRING; 1110502.TMO_0649; -.
DR KEGG; tmo:TMO_0649; -.
DR PATRIC; fig|1110502.3.peg.674; -.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_000445_107_12_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF02743; dCache_1; 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.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
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 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..421
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 454..690
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 623..675
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 75882 MW; 1232DB02C7833250 CRC64;
MAAAARGLRI VHKIPGAIVA AVAITSIVLG VVAYLVSSRE LVEASETKLE AITEGRKARL
NDYLERVRSD VAVLADNSVL RQTLIDFTYA FELISLMDDK PDQILQKSYI TDNPETDRAV
LNKAGDGTFF SDSHERYHPW LRAASRSKGY ADLYLVDKNG WVVYSVEKNT DFAVKLDESD
VGQTGLGRAV AAAQAATEPG QVSLIDFTYH PQANNEVSAF LAVPVFGDGG YVGAVVVRLS
VNGVDNVMQS AQGLGETGET YLVGSDGYMR SNSRLSADTT VLERQVNTDA VAAALAGKSG
SVRDVGPGGY AVLSAYQPLE FLGQRWAVIA DVAEDEILAP VVDMRNMIAA VAVGLIVIVG
SIGMLVARGV TRPLGRMTGA MKELSNGNLS IDIPDRDRSD EIGEMAASVQ VFKDAMVESQ
RLAEAQRLDQ EEKSKRAEEL VRLTRGFDDR VSGVLRGVTA AATELDATAR SMSSTADGAR
HQSDEVAHAT AQATENVQTV AAAAEELSHS ISEIGRQVHK SSTIAGRAVD EAERTNQTVY
GLAAAAEKIG DVVRLITDIA EQTNLLALNA TIEAARAGEA GKGFAVVASE VKSLANQTAR
ATEEISTQIA AVRGETNQAI GAIEGIRKII VEINDIATSI ASAVEQQSAA TQEIASNVQA
AARGTEQVSR SVDDMRDAAQ ATGSASQQIL SSAGELARQA TDLDSEVRSF LEAVRAG
//
