ID S6AG73_SULDS Unreviewed; 1186 AA.
AC S6AG73;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SCD_n01147 {ECO:0000313|EMBL:BAN34981.1};
OS Sulfuricella denitrificans (strain DSM 22764 / NBRC 105220 / skB26).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuricella.
OX NCBI_TaxID=1163617 {ECO:0000313|EMBL:BAN34981.1, ECO:0000313|Proteomes:UP000015559};
RN [1] {ECO:0000313|EMBL:BAN34981.1, ECO:0000313|Proteomes:UP000015559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skB26 {ECO:0000313|Proteomes:UP000015559};
RX PubMed=22773644; DOI=10.1128/AEM.01349-12;
RA Watanabe T., Kojima H., Fukui M.;
RT "Draft genome sequence of a psychrotolerant sulfur-oxidizing bacterium,
RT Sulfuricella denitrificans skB26, and proteomic insights into cold
RT adaptation.";
RL Appl. Environ. Microbiol. 78:6545-6549(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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP013066; BAN34981.1; -; Genomic_DNA.
DR AlphaFoldDB; S6AG73; -.
DR STRING; 1163617.SCD_n01147; -.
DR KEGG; sdr:SCD_n01147; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3452; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_289488_0_0_4; -.
DR Proteomes; UP000015559; 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 CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000015559};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 137..280
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 325..392
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 399..451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 452..530
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 576..620
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 648..695
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 768..820
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 893..943
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 972..1186
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 934..965
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1186 AA; 132835 MW; 1E65ABDA34091F37 CRC64;
MGGSGSRLPQ EMQTYSRRFH TAGYVRVILA TGYRFFGEKA RPWLFALLAV LLVLATEQVV
EHFARQSDLE QERNDVLNRL STLRARLEGV INANLFLVHG LTAVIENRPD IDQAGFSAIA
SNLVDERHAL RNIAAAPDMV ISLMYPLQGN EAALGLDFRT HPTQRESALR ARDSGKTVIA
GPLSLQQGGI AIIVRKPLFL VPAQSGGKRH FWGLVSAVID AETLYRMAGL RDPDLGLRLA
LRGTDGTGSH GPVFFGDAKL FGNQSVTLDI TLPGGSWQMA ATPVDGWEQV GMSIILFRLM
GLLTALAAGI MVNRLVRDSQ ALVSHSAKLR ALLNTIPDMI WLKDAHGVYL TCNPRFEQLF
GAREVDIRGK TDHDFVPADL ADFFREKDLA AITAGGPSTN EEWVTFASDG HRELLETIKT
PVYDNKGDVL GVLGIARNIT ERQRQEEEMK RLHATLHALV EGSTDAIFVK DREGRYVVGN
QATATLLGRP MAEILGADDC NLFPAEVAES FQSDDRRVMQ RGATETYEEA VVVEGKTLPY
LTTKGPLLID GKVEGVFGIA RDISPLKQSE IAVRESEARY RTLFEYAPDG IVIADQESYY
LDANPAICRM LGYNREELIG LHASDIVVAA ELTNIVPALE VIKGKKDYQR EWQFRRKDGS
TFVAEVIATT MPDGNLLGVI RDITERKQAE AALQESETRL RLFIEHAPAA LAMFDREMRY
LVVSRRWLTD YSLEGSNILG RSHYEIFPEI SERWKTVHRR GLAGEVVRAD EDRFERGDGT
VQWLCWEVRP WHAADGAVGG IVIFSEDITE RKQAEQVLQE SEARYRSLLE MAPFPAVLSR
LRDGILLYGN HRAEIQYGIS REQGIGQPAD RFYQNPAQRD RFIEHLRKDG RVDDLEVGMV
TMDGRPFLAL VSASIVNFEH EPAVFAAIND ITARKRMEDD IRQLNDELEE RVRQRTAELD
TANQELETFT YSVSHDLKAP LRGIDGYSRL LLEQYQTLLD EEGRLFLNNV RHGVEQMSLL
IEDLLVYSRM ERRSLTGQSV DLARLVVGVL DERRKDIEAR GMIVEAQGLQ ELPVRADPEG
LAMVLRNLVD NALKFTRDSK PPTLTIRGTA SEKSVILKLH DNGIGFDMQF HDRIFDIFQR
LQRVEDYPGT GVGLAIVRKA MQRMGGRVWA ESAPGQGATF YLELPR
//