ID A0A2R8BH87_9RHOB Unreviewed; 827 AA.
AC A0A2R8BH87;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Methyl-accepting chemotaxis protein III {ECO:0000313|EMBL:SPH22387.1};
GN Name=trg {ECO:0000313|EMBL:SPH22387.1};
GN ORFNames=ASD8599_03130 {ECO:0000313|EMBL:SPH22387.1};
OS Ascidiaceihabitans donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Ascidiaceihabitans.
OX NCBI_TaxID=1510460 {ECO:0000313|EMBL:SPH22387.1, ECO:0000313|Proteomes:UP000244880};
RN [1] {ECO:0000313|EMBL:SPH22387.1, ECO:0000313|Proteomes:UP000244880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8599 {ECO:0000313|EMBL:SPH22387.1,
RC ECO:0000313|Proteomes:UP000244880};
RA Keele B.F.;
RL Submitted (MAR-2018) 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; OMOR01000001; SPH22387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8BH87; -.
DR Proteomes; UP000244880; 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; 6.10.340.10; -; 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; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000244880};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..421
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 513..565
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 570..799
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 807..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..453
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 827 AA; 88608 MW; AA6F29469ADA27B2 CRC64;
MKNPIRNIAI GVKLPIAIAC SVAITVIALT IVSVTAARGI IANSVEEKLE SIAMMQADRV
NDLFGSIERD IRLQSATPLI AQALVAFTDG FESLGEDAYE TLTRVYIHEN ENPTGQKDLL
VKADTQSSYG FMHSIYHPVL DNLQNEMGYY DVFLFDVKGN LVYSVFKETD FATNFVDGMW
KDTGLATAFS KALERTPDQE TVYVDFSRYG PSHSVAAAFM SRPVVDQNGI LVGVLAYQMP
VAALNQAAGD LQGLGATADG FLIGDDHLLR SSSIQTNETD ILELAHNGEI ITRGLTGQGG
GFSDTGFNSQ GVMGYFNPIE FLGTKMVAIV QQDTKELFAG VGPLVFKILL FSLAIFLTVL
MAAIMFSRSI SVPIKNLTNS VKDVAAGNLQ TNVPETTRGD EIGSLARATE VFRQNALKID
ALNAEQTRAN TKMEQLNTER ESAAQREALL ASEKIEADKS AAAERQEMVE ILGQSIGQVV
TEAIAGNFSK RIEAQFDDQT LVALSNDINA LMQAVDSGLT ETGRLLERVA QGDFSQRMTG
RFDGAFADLQ RNVNDMIDAL TSLIVDIADT GETLAISSSE MQETAQALSQ RAEDNAASVE
ETSSALEHLS SSVRQVRDNV HEASADATEA RKTAASSEKI AAEAVSSMDR IAEGSREITR
VVAVINEIAF QINLLALNAG VEAARAGEAG RGFSVVASEV RALAQRASEA ATEIEGVISA
SDIAVTDGVS KVGSARNLLE HIAARVVAIS DRVEVVTAAV SEQSKGIDEI STAAIAIEQN
TQKQAASLEE VTASTLELAS QSRDLKKSTA RFQIEAPNHN QNNRKAG
//