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Database: UniProt
Entry: A0A017RWV8_9CLOT
LinkDB: A0A017RWV8_9CLOT
Original site: A0A017RWV8_9CLOT 
ID   A0A017RWV8_9CLOT        Unreviewed;       580 AA.
AC   A0A017RWV8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Q428_08025 {ECO:0000313|EMBL:EYE88420.1};
OS   Fervidicella metallireducens AeB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Fervidicella.
OX   NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE88420.1, ECO:0000313|Proteomes:UP000019681};
RN   [1] {ECO:0000313|EMBL:EYE88420.1, ECO:0000313|Proteomes:UP000019681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AeB {ECO:0000313|EMBL:EYE88420.1,
RC   ECO:0000313|Proteomes:UP000019681};
RX   PubMed=24786951;
RA   Patel B.K.;
RT   "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT   Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL   Genome Announc. 2:e00345-14(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:EYE88420.1}.
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DR   EMBL; AZQP01000021; EYE88420.1; -; Genomic_DNA.
DR   RefSeq; WP_035379740.1; NZ_AZQP01000021.1.
DR   AlphaFoldDB; A0A017RWV8; -.
DR   STRING; 1403537.Q428_08025; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000019681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR031967; PhoR_single_Cache-like_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF16736; sCache_like; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EYE88420.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019681};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          182..234
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          239..276
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          360..576
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   580 AA;  65884 MW;  392EE1282E64A65C CRC64;
     MRKRLFSFFI IILFLGVVIT GTLSYNSTRK IVLKNLKKSL REECNLSADY IIFKGNTSDF
     DSIANDISKK LNKRVTIIRD DGKVMGESLY AHQYLDNHLG RPEIRDALKF GEGVSTRYSN
     TEKTLKFYYA KKFEASGQIF IVRLAMELND IKDMQGSYLR LILIAMFVGV VVCSLLAFVY
     LNKITKPIRQ LTSVATTISL GDYERRINIT SNDEIGQLGH AFNIMAGRLE ETIVDLSDKR
     TKLISILKSM DDGVIVVDNN EKVLLINPAA QKLFNIGENV AGKHFIEVIR SYDIEDIIRN
     IPDEDTEITI TYPVTKYLRI KATKVTNYDS NKESIGVMLF IQDITKIKSL EKMRSDFVAN
     VSHELKTPLT SIKGFSETLK YVEDKETRDK FLDIIYVESE RLTRLINDIL SLSELENKNI
     SLNLEKIDVF DTLDEVFHIM EYAAKEKNID LEMNCQEDSL FINGDRDKFK QMIINLVDNA
     IKYTNPHGKV LIKGEGENGK VKISISDNGI GIPEVHIPRL FERFYRVDKA RSRDAGGTGL
     GLAIVKHIVM LLNGDIQVKS KVGEGTTFTI YLPVINSELT
//
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