ID A0A1H2YJ92_9RHOB Unreviewed; 750 AA.
AC A0A1H2YJ92;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SDX05312.1};
GN ORFNames=SAMN05444336_103152 {ECO:0000313|EMBL:SDX05312.1};
OS Albimonas donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=356660 {ECO:0000313|EMBL:SDX05312.1, ECO:0000313|Proteomes:UP000199118};
RN [1] {ECO:0000313|EMBL:SDX05312.1, ECO:0000313|Proteomes:UP000199118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17890 {ECO:0000313|EMBL:SDX05312.1,
RC ECO:0000313|Proteomes:UP000199118};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNMZ01000003; SDX05312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2YJ92; -.
DR STRING; 356660.SAMN05444336_103152; -.
DR OrthoDB; 369026at2; -.
DR Proteomes; UP000199118; 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; 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; IPR032255; HBM.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN II-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM01358; HBM; 1.
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:UP000199118};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 319..372
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 436..488
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 493..722
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 535..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 505..532
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 750 AA; 79183 MW; 30AE2DCDF526A136 CRC64;
MLARFSIFQR IVGGFGGALV VILGLAAFSY QSTSRLGHDF GEVRDATNDK AAIDLLSIDL
YAMRQEGFRY FAAANPELLK PMAARRTAIV EHVAAAKEAV ENDPALSGAL DRFAAGSSRY
VDLFEQLSAM DVERDAIRNE ALDAAQAARD AFDLVRDTAL ERGENLAAAQ AGRAIEEIIK
STRLLIVYAD TGVEADHDAW FETLNEMQTD GKRAFDEAAR SGLRPMAELA VAAMADLTRH
VQPLADVIAR RTTLFFEEIA PLGPELNETI EAVQNQVSAR RAGILDAADK EVASATMVVI
LSGLVGAGLA VALSLVIGRS ISSDVSQTTR DMQRLAGGDV GFDIHGVEHT HEVGKMARAL
GVFRDNQLAL ARTEKERVEA EAEAARKRAA MMKELQDNVG AVVDAAVAGD FARRVEARFD
DAELAALASG VNRLLGSVQG GLDAARRAMS DVASGDLDTA MRGDFKGAFG ELKRDVDATV
TRLRGLVEDI RNGSANIVTV AAAMSDDAEH LSQSAESQAA SLEETAATME EISSTVRRNA
ENSKEAANLS RQASKSASSG SQVVGDTVEI IERIEASSSR IADITSVIDG IAFQTNLLAL
NAAVEAARAG EAGKGFAVVA AEVRQLAQRS ADAASDIKRL IEDSGRQVSE GVDAAKRAGE
SLEEIVSAVT RLEQTIDDIS AASMEQSAGI DEISSAVASL DQATQQNAQM AQDAARRTGE
MTGTARGLQD RVDAFVGASD AGGARSARAA
//