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Database: UniProt
Entry: A0A1G3E1H8_9GAMM
LinkDB: A0A1G3E1H8_9GAMM
Original site: A0A1G3E1H8_9GAMM 
ID   A0A1G3E1H8_9GAMM        Unreviewed;       433 AA.
AC   A0A1G3E1H8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=A2Y50_06475 {ECO:0000313|EMBL:OHC25790.1};
OS   Pseudomonadales bacterium RIFCSPLOWO2_12_59_9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales.
OX   NCBI_TaxID=1802009 {ECO:0000313|EMBL:OHC25790.1, ECO:0000313|Proteomes:UP000179365};
RN   [1] {ECO:0000313|EMBL:OHC25790.1, ECO:0000313|Proteomes:UP000179365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHC25790.1}.
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DR   EMBL; MHZN01000290; OHC25790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3E1H8; -.
DR   STRING; 1802009.A2Y50_06475; -.
DR   Proteomes; UP000179365; 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; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 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   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        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..155
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          160..396
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OHC25790.1"
SQ   SEQUENCE   433 AA;  44984 MW;  104B20264CE3E459 CRC64;
     DRSLQEKLTA FVSDAGQSAR DATELARSKV AALDSLAYPA PEYIAFFTQA IDVQYQLVNA
     AMQQLDEHIA ARIAKQRSAR NGLVAGISLI AGLALAIGWR VAASILRPVA QALAAAQAVA
     QANLAAPIAG GGRGETGQML SALAQMQQAL HKTISITRQH ADDLANAAEA LAGSSNQVSQ
     ASSRQSDSSA AMAAAVEELT VSIGHVSNNT GEAGRASVNA KQLSQEGVEA IQKAAGEIRT
     IAASIRLTAK MISELGEHSQ RISGIVEVIR GVADQTNLLA LNAAIEAARA GEQGRGFAVV
     ADEVRKLAER TSGATQEIAQ MIEHIQTRTA EAVAGMAQAV DQVGGVEVST EQAREAVDRI
     TASTRLVEDA LLVIDTTLKE QSSASNEIAA RVEQVAQMSE ANSAAATEAA EAAQTLTQLA
     TAMRAEVAHF RLS
//
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