ID H1G5D3_9GAMM Unreviewed; 615 AA.
AC H1G5D3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Chemotaxis sensory transducer {ECO:0000313|EMBL:EHQ53020.1};
GN ORFNames=ECTPHS_10044 {ECO:0000313|EMBL:EHQ53020.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ53020.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ53020.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ53020.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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:EHQ53020.1}.
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DR EMBL; AGBG01000022; EHQ53020.1; -; Genomic_DNA.
DR AlphaFoldDB; H1G5D3; -.
DR STRING; 519989.ECTPHS_10044; -.
DR eggNOG; COG0840; Bacteria.
DR Proteomes; UP000005314; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
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; IPR029150; dCache_3.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF14827; dCache_3; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 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 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 255..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..330
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 335..571
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 367..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 67074 MW; 5998BAD15E55248F CRC64;
MEQNGHYLAT MLEERLQSKR EFGIGVSVML AEHPDIRDAY LLDDRDRAHQ AIRDILETFR
TTTNYRGLRV QVHTGDGASW QRSWAPDQYG DDLSFRASIQ EMLRTQRPIA EGNEMGRAGY
AIRALAPIME NGVYRGSLEL LQGVGSISRD FEAEGAAYVL LLSPTALENS PGIAGNRRVG
EYFVANDNWF NQYAMEFANS LDLDRLVNDG LDIGRDWFGV QVPLVNDRGE QIGMHVIGMR
ADAVREQIVS ATRSAWMFLG LIAALVIIMG LVIAWLVQRG MVGPIRAGVE RIRQMEHDSS
LRLEVRGKDE LAVLSQAFNH YADNLQDILQ QISGTSTSLG GAAEELVNHS RQGLDLVRQQ
QQETQQVASA SVEMAASAGE MSQHAQSTQD AAGEALSSAE NGIRLVGETA NAIEALATNM
RGMLDVIQRL DQGSQSIGKV LETISEIADQ TNLLALNAAI EAARAGEHGR GFAVVADEVR
KLASKTQNST SEIYGIIKDV QNSVSDVTAA IHRGQGEAET CVSHAQEASG SLGSIKKAVK
DVHEQGIHIA QSAREQNHVA EEVSRNIVRI NTLADDNGRA AEQILDIAQG LEQSAEALDR
MLTANRLVRL AEIGH
//
