ID A0A0D7K9H5_9BURK Unreviewed; 551 AA.
AC A0A0D7K9H5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KJA10970.1};
GN ORFNames=RP29_08055 {ECO:0000313|EMBL:KJA10970.1};
OS Acidovorax temperans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA10970.1, ECO:0000313|Proteomes:UP000032566};
RN [1] {ECO:0000313|EMBL:KJA10970.1, ECO:0000313|Proteomes:UP000032566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY4 {ECO:0000313|EMBL:KJA10970.1,
RC ECO:0000313|Proteomes:UP000032566};
RA Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT "Isolation of bacteria from lake water.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:KJA10970.1}.
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DR EMBL; JXYQ01000022; KJA10970.1; -; Genomic_DNA.
DR RefSeq; WP_044397190.1; NZ_JXYQ01000022.1.
DR AlphaFoldDB; A0A0D7K9H5; -.
DR STRING; 80878.RP29_08055; -.
DR PATRIC; fig|80878.5.peg.1130; -.
DR OrthoDB; 9151832at2; -.
DR Proteomes; UP000032566; 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; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN II-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF12729; 4HB_MCP_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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032566};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 196..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..270
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 275..504
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 532..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..520
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 551 AA; 58373 MW; 1531B12A9C71980C CRC64;
MNLFSLMRQF TIRFRMLGAI AVVLVLLGLL GGAGMFGMFR IYSMSEDFMN SSFQEVGYLA
QLHSEMGAIR QHEKDMIIGY EKPEAVKAAH TQWLESQEKA KKVANQFLQG EEDVDNAVVR
DIIKRLDSYK EAFAHVARQL EAGGYDTTTI ANRMSGKAVA EFAEADKLMK QLDEVLRNEV
QKSVAEQQGV SNQTKWLFAL AVLITVVVVV PLTLLNMHSI CKPLDQAQRL AKAIAGGDLS
QSIRTEGRDE VADLLRALDE MQRGLGTLVA QVRDASGNIA TASQEIATGN QDLSHRTELT
ASNAQAAVSS LSEITATVQQ TASSSQMANQ LAASASTTAT RGGSVVAQAV SSMHEIAASS
RKIGDIIGLI DSIAFQTNIL ALNAAVEAAR AGEQGRGFAV VASEVRSLAQ RSAAAASDIK
VLIQSSVTAV DGGVRHVEDA GTAMKDIVSS VQRVGDIIGE ITAAASEQSA GIGQVNQSVA
EIDRMTQQNA ALVEESAAAA ESLREQAARL SQVVQQFRLA DSMGFAGHGS FSAPAPQGLS
APSSAPRALL G
//