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Database: UniProt
Entry: A0A1I4W7H3_9NEIS
LinkDB: A0A1I4W7H3_9NEIS
Original site: A0A1I4W7H3_9NEIS 
ID   A0A1I4W7H3_9NEIS        Unreviewed;       540 AA.
AC   A0A1I4W7H3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SFN09581.1};
GN   ORFNames=SAMN05660284_00492 {ECO:0000313|EMBL:SFN09581.1};
OS   Formivibrio citricus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Formivibrio.
OX   NCBI_TaxID=83765 {ECO:0000313|EMBL:SFN09581.1, ECO:0000313|Proteomes:UP000242869};
RN   [1] {ECO:0000313|Proteomes:UP000242869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6150 {ECO:0000313|Proteomes:UP000242869};
RA   Varghese N., Submissions S.;
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; FOVE01000003; SFN09581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4W7H3; -.
DR   STRING; 83765.SAMN05660284_00492; -.
DR   OrthoDB; 9179351at2; -.
DR   Proteomes; UP000242869; 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; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 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; IPR024478; HlyB_4HB_MCP.
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; PF12729; 4HB_MCP_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000242869};
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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..263
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          268..504
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   540 AA;  58128 MW;  51FFE0799D475101 CRC64;
     MGIANRIIMI LTIALLSLLG VGGYALWGLG AAQTRFEYVQ ENTVPSVKAL DEARVSVDQI
     RIAVRDHLLA ENTAEKEAAE KHIAEHYQLA LKNLNRYEKE LLSDDTDKKM TEADKASLAR
     YMSIVKTLLQ KSDAKDTHGV HVMLLPTGEF SQTARGLTKN LADHMDYNWK LAEGLRKDNA
     AAYARAKWIQ VSAILLALAV VGTLGYLVAK EIRFRMNRLQ DMMKQVNQSL DFTLRIPVAR
     LDELGASADA FNKLLERLQG NLRSVAAGAQ SVAAAANQMA TTSTQVARAS QQQSEAASGM
     AATVEEMTVS INHVADRAQE ANRISSESGK LANMGEQVIG QTASDIQDIA TTVNEAADLI
     HSLEQHSQQI SNVVSVIKEV ADQTNLLALN AAIEAARAGE QGRGFAVVAD EVRKLAERTA
     SSTQEIASTI DTMRNSAGNA VASMQGVVAK VGKGVEQAQV ANDSIRQIGE GSRNAVGMVE
     EITTAIREQG TATNNIAIQV EKIAQMSEES SAAAEESARA AHDLDRLAGE MHDIVAAYRL
//
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