ID G2G2P7_9FIRM Unreviewed; 557 AA.
AC G2G2P7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=HAMP domain protein {ECO:0000313|EMBL:EGW35851.1};
GN ORFNames=DOT_6288 {ECO:0000313|EMBL:EGW35851.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW35851.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW35851.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW35851.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
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:EGW35851.1}.
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DR EMBL; AGAF01000281; EGW35851.1; -; Genomic_DNA.
DR RefSeq; WP_009624943.1; NZ_AGAF01000281.1.
DR AlphaFoldDB; G2G2P7; -.
DR PATRIC; fig|913865.3.peg.5781; -.
DR eggNOG; COG0840; Bacteria.
DR OrthoDB; 5392220at2; -.
DR Proteomes; UP000004928; 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 Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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 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 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 256..528
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 557 AA; 59509 MW; FFF5A7E68A08FCC8 CRC64;
MKLATKLLLS FIALISLMSV IVGEVYYEVD MLGGIVQKAA THRVPMQTTA QDLSLQFSQQ
AAGIRGYLAT GNEKFIQDFQ NAKIMGDKDL QFLQTEATDK EKLAPVVTAI SKFSPHPQKM
VDLYKTQGQA AAIEYMVNIA AHDNTAAIQA INDYVAYQRH QMSSETSDTP LMVRKVISIT
LILFGIAVII SIAVLIYIRR SVKTSISKGL VLAEAMAEGD LSIEVQGSKD EIGVLVTNLS
KAAQMLRAMV KKSAAVTQDI NQAASDSTEA VTNVASSSQE MAASTEQVAA GLQEIAAAAE
EITASSDELK NSIRQLEESA SSGNMQAMAI DKRAKDLKQE AIQAQIKAQG IYEKEEEALK
KAIEESKVVQ EIAALTKGIS AIADQTNLLA LNAAIEAARA GENGRGFAVV AEEVRKLAEQ
SSQTVKEIEQ LVGKVIKAQE DLSVGAQNSL RFINDVVAPD YSKLLETGSQ YEQDADTVLN
LTNGFSNMSK NLAEVVNSIA IAITSVTQTI SEGAAGAEEV AGASAGISID LEKVNHAMVQ
LSGNATELSE VVSKFRV
//
