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Database: UniProt
Entry: E4U1L0_SULKY
LinkDB: E4U1L0_SULKY
Original site: E4U1L0_SULKY 
ID   E4U1L0_SULKY            Unreviewed;       654 AA.
AC   E4U1L0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Sulku_0780 {ECO:0000313|EMBL:ADR33446.1};
OS   Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 /
OS   YK-1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfuricurvum.
OX   NCBI_TaxID=709032 {ECO:0000313|EMBL:ADR33446.1, ECO:0000313|Proteomes:UP000008721};
RN   [1] {ECO:0000313|EMBL:ADR33446.1, ECO:0000313|Proteomes:UP000008721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1
RC   {ECO:0000313|Proteomes:UP000008721};
RX   PubMed=22675602; DOI=10.4056/sigs.2456004;
RA   Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M.,
RA   Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S.,
RA   Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of the sulfur compounds oxidizing
RT   chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)).";
RL   Stand. Genomic Sci. 6:94-103(2012).
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};
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DR   EMBL; CP002355; ADR33446.1; -; Genomic_DNA.
DR   RefSeq; WP_013459643.1; NC_014762.1.
DR   AlphaFoldDB; E4U1L0; -.
DR   STRING; 709032.Sulku_0780; -.
DR   KEGG; sku:Sulku_0780; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_027703_0_0_7; -.
DR   Proteomes; UP000008721; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.60.40.2380; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ADR33446.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008721};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:ADR33446.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..654
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003189975"
FT   TRANSMEM        177..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          431..645
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   654 AA;  75719 MW;  D8ED93691D84C132 CRC64;
     MFFRIILPFI FYVSSSFASI VIAENTDQIS KFSIPYVYDE KSLLSVDEIA DKNFTQTVPS
     QFSFGYKDGT VWFKLTIENK SRDNDFILYF GEPFWSTFNL YEPTESGWVK HSAGLLTHLN
     ERQIEDANPT FRLTIAPGMS KTYFLQGQTI NAQIGAFTLY SEKEFFRPSR LTLRTFYPFY
     SGILFIIMIL NIFLLVEMRE RIYAYYIGYV SSFIAFVTMF NGCYLYIGFH PWEQGLHVVG
     TVVLAFMALF SKTFLELEKY FPKMNRLFKL FAVSFLTLGV LIHLEIPLAT LFFNILSTVF
     ITILLTLAVK IWQNGKMQTP FYLIALMIYM PTMGMMVLTF NGFLENTDIN RYAFLFGALI
     EIIFFALILA QRFHAAKDEK IQLQKELLIE KEKNQEYLEH KIDKQRQEIK EKNAILFHQS
     RHAAMGEMIS MIAHQWRQPL NTLAIIIQNL YFQHKLGQWD EGNFEQSHDQ FNEHLQYMSK
     TIDDFRNYYK NDETKRPENI GEIVELALRL CDVFLKYAKI KTTLTISTDK MGYLSKNELT
     QVLMNLIKNA HDAIVERGIH PGKITILVEE TDGSIAINVC DNAGDISGAI ADKIFEPYFS
     TKSENGTGLG LYMSKSIIED HFHGALTFQN IDAGTCFTIM IPIYDKSMEE DKTP
//
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