ID H5YNA1_9BRAD Unreviewed; 560 AA.
AC H5YNA1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:EHR05703.1};
GN ORFNames=Bra471DRAFT_06531 {ECO:0000313|EMBL:EHR05703.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR05703.1};
RN [1] {ECO:0000313|EMBL:EHR05703.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR05703.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; CM001442; EHR05703.1; -; Genomic_DNA.
DR RefSeq; WP_007614601.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YNA1; -.
DR HOGENOM; CLU_000445_107_21_5; -.
DR OrthoDB; 8482111at2; -.
DR Proteomes; UP000005774; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 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; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
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; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF17200; sCache_2; 1.
DR SMART; SM01049; Cache_2; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
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 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..263
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 304..526
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 456..518
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 560 AA; 59161 MW; 5F146CA6646D9319 CRC64;
MFFSRISFKL VLIVGISLLG MIALAPIALS TLRTQMIADR EAKTQHMVDV GYGILAHYQK
LESEGKLPRE QAQAGAIAEI KSLRYDKVEY FWLNDMTPKM VMHPIKPELD GKDLAGMKDP
AGNALFVGFV DVVKKQGAGF YSYLWPKPGF DQPVGKISYV KGFAPWGWII GTGIYLDDVD
AVFRQNAMTF ALVCLVVLVL VLGASFVIGR SVTRPLAKIT ALTDRLAAGD SAFDVPHTDR
RDEIGGLAKA LAVFKDNASA VGRMHAEQQE TKQKADEEKR KTMTDLAGKF EANVQAVVRD
VFNEARAMQQ AAQGMSATAD KATDRASFVA TACQQASSNV QTVASAAAQL SSSITEISQR
VAQAASVADK AAADGQRTND TVQGLAAAAH KIGEVIDLIN QIASQTNLLA LNATIEAARA
GEAGKGFAVV ASEVKSLASQ TAKATDEIGA QITAIQAETN QVVGNIDSIR KTIMEVNEIS
SSIAAAVEEQ GAATAAIAHS VREAASGTDQ VSQNISGVTD ATAETGQAAG LVLQSSGRLS
QKLQSLENEV SAFVAGVRAA
//
