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Database: UniProt
Entry: A0A0U5CXF7_9EURY
LinkDB: A0A0U5CXF7_9EURY
Original site: A0A0U5CXF7_9EURY 
ID   A0A0U5CXF7_9EURY        Unreviewed;      1080 AA.
AC   A0A0U5CXF7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Transducer protein Htr39 {ECO:0000313|EMBL:CQH54488.1};
GN   Name=htr39 {ECO:0000313|EMBL:CQH54488.1};
GN   ORFNames=HHUB_2091 {ECO:0000313|EMBL:CQH54488.1};
OS   Halobacterium hubeiense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH54488.1, ECO:0000313|Proteomes:UP000066737};
RN   [1] {ECO:0000313|Proteomes:UP000066737}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX   PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA   Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA   Yang C., Oksanen H.M., Bamford D.H.;
RT   "The complete genome of a viable archaeum isolated from 123-million-year-
RT   old rock salt.";
RL   Environ. Microbiol. 18:565-579(2016).
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; LN831302; CQH54488.1; -; Genomic_DNA.
DR   RefSeq; WP_059056532.1; NZ_LN831302.1.
DR   AlphaFoldDB; A0A0U5CXF7; -.
DR   STRING; 1407499.HHUB_2091; -.
DR   GeneID; 26658754; -.
DR   KEGG; hhb:Hhub_2091; -.
DR   OrthoDB; 8523at2157; -.
DR   Proteomes; UP000066737; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd11386; MCP_signal; 1.
DR   CDD; cd18774; PDC2_HK_sensor; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 2.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066737};
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        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          544..597
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          680..732
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          751..987
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          1042..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          717..747
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          822..856
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1046..1060
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1080 AA;  115318 MW;  09F66FE27912BFEC CRC64;
     MKIRTKLIAL CLVISLVPVS AVGVTGLQNM ESVGSYAQQE STTQLEDQIT GELNGTVHSR
     QAEFQNLLNV RSVDARSLSE STPVQNYEAA NAGEMELIRE QSQRQVGYVA LQMHSTVETT
     KQQLLDDQYD GQSWGALSAS EQQAVKDEVE QRLFGTSGDF TQSSGTLAEA MQPGYIGDTG
     YAYVTDLDSR VVAHHSLEDG YSLREDAGLT VFDDIGSTVE SDEAIRNGEE WGVAEYGWED
     TTQAGNPVEQ KFIAYTYHED FDWVLAPNVY YYELQTSAVA DARDGIRDSF RSYMESRTVT
     VGDEERPAYD EIVLTDDTGD GVVRAHRTAD GTVATETVKD TSYADTDWYA ETESLPNGEV
     HVSDVQTVDG EQVVYIATPV YYDGEVAGVV SLRFDYSIIS DIATDITVGD SGYLSVVAGD
     GTVLSHPNES VVASGASITS ESYGGTLAGD AANTVLAGDT GLRTFERTAA DGSTERFYAA
     YAPLEFGDRQ LALLGTVPAT DVTGPADALA AAVDSRTTDA RNLLLLLVAV VIVAVVALGY
     YAARYFSRPI EAVRDQATAL SQGRFEDGTD VDAPDDEIGE LVDAFEDMRR NLRRQVAQLR
     DVSTGLEQGE LDQDVDTDLP GEFGAIMTEL DGGIDRLQVG FDEIRATSGR IREGDLDSDV
     DTDLPGEYGA VLTDLDAGVQ QLSGSFDQLG EVSRQLREGD LDQDIDTDLP GQYGEVMVDL
     EAGVEELEAS LAEVREVAEK FAELSDETAA SAEEIKSASQ ETAQAVEQIA SGADQQTEQL
     QSVSHEMNDL SATIEEVASS SEDVVATANE AVELADRGRD HAADATDEIS AIESEADEAV
     QQVEELDDQI EEINEIVGLI TDIAEQTNLL ALNASIEAAR AGEAGEGFAV VANEIKTLAA
     EAGDATDEVE ALIDEIQDST DATVEDMQSM QHRVETGSET IAGAIEMFDD IAEAVTDAGR
     GVEEISDATE DQAVSTEEVV AMVDEVSSVS EESAAEASNV SAATEEQTAA IDEVTTNIQN
     VSQSAQSLQT LVAQFDVADD AGTAGESYEP SEREFDFDAD GADQGAATDG GNADADPADD
//
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