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Database: UniProt
Entry: A0A285KBF2_9ENTR
LinkDB: A0A285KBF2_9ENTR
Original site: A0A285KBF2_9ENTR 
ID   A0A285KBF2_9ENTR        Unreviewed;       532 AA.
AC   A0A285KBF2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer with TarH sensor {ECO:0000313|EMBL:SNY69930.1};
GN   ORFNames=SAMN02744775_02250 {ECO:0000313|EMBL:SNY69930.1};
OS   Enterobacter sp. CC120223-11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=1378073 {ECO:0000313|EMBL:SNY69930.1, ECO:0000313|Proteomes:UP000219512};
RN   [1] {ECO:0000313|EMBL:SNY69930.1, ECO:0000313|Proteomes:UP000219512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC120223-11 {ECO:0000313|EMBL:SNY69930.1,
RC   ECO:0000313|Proteomes:UP000219512};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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; OBEF01000008; SNY69930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285KBF2; -.
DR   Proteomes; UP000219512; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd19407; Tar_Tsr_sensor; 1.
DR   Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR035440; 4HB_MCP_dom_sf.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR003122; Tar_rcpt_lig-bd.
DR   PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF02203; TarH; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 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   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Transducer {ECO:0000256|PROSITE-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        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          227..281
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          286..515
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          294..321
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   532 AA;  58001 MW;  724EAC195D9DE3BB CRC64;
     MKIMNLMQIP RRFVRRFFPQ QFGLLAGVFT IVGLFCALQI ASSFMLSWSL HNARLNEQHN
     QRAHMQQLEA DRARVNLLAA SDLLNRAGVY FMQDRETGSV GSSEGLLQDA RASLVLSQKA
     WQAWLAMTPP RDEALINSYQ QFYGAIEEQL NGLQKSQSID AFFAVPVQAF QADFNDNYAR
     FQAASESLAG KGRESLMASL AGLQQLFMLA PVALLIVALL VWRGMSHWVI VPLRRLIDHI
     RTMAEGDLSQ PLPQVSRRNR EVAQIGATLA EMQVGLQQLV AEVSEATGSI TGNITRLAQS
     NEELSRQAHK QTQELEDVTR HITSLESHVE GNAGYAGLAR ERAEEASLAA AGGDRMMLTV
     NASMQAIVAR SAEMRGIVAM IDSVAFQTNI LALNAAIEAA HAGNQGRGFA VVAKEVGLLA
     RQSSESTQTI QGLINHSLQG IEEGSQAVGR LEDNLQKVTN LVTNLSALLT EISQATLNQG
     ENIHQMTQQL HSLNQVAGKT GELVSASAAS SRHLESSAGL LMQAVMRFRL PA
//
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