GenomeNet

Database: UniProt
Entry: D1B1H3_SULD5
LinkDB: D1B1H3_SULD5
Original site: D1B1H3_SULD5 
ID   D1B1H3_SULD5            Unreviewed;      2035 AA.
AC   D1B1H3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Sdel_0913 {ECO:0000313|EMBL:ACZ11943.1};
OS   Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurospirillaceae; Sulfurospirillum.
OX   NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ11943.1, ECO:0000313|Proteomes:UP000002222};
RN   [1] {ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Munk A.C., Lu M., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Aumann P., Schneider S., Lang E.,
RA   Spring S., Klenk H.P., Eisen J.A.;
RT   "The complete genome of Sulfurospirillum deleyianum DSM 6946.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ11943.1, ECO:0000313|Proteomes:UP000002222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51133 / DSM 6946 / 5175
RC   {ECO:0000313|Proteomes:UP000002222};
RX   PubMed=21304697; DOI=10.4056/sigs.671209;
RA   Sikorski J., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., Goodwin L.,
RA   Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Detter J.C., Han C., Rohde M., Lang E., Spring S., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Sulfurospirillum deleyianum type strain
RT   (5175).";
RL   Stand. Genomic Sci. 2:149-157(2010).
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; CP001816; ACZ11943.1; -; Genomic_DNA.
DR   RefSeq; WP_012856707.1; NC_013512.1.
DR   STRING; 525898.Sdel_0913; -.
DR   KEGG; sdl:Sdel_0913; -.
DR   eggNOG; COG0642; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_233355_0_0_7; -.
DR   OMA; MIHESAG; -.
DR   OrthoDB; 5468627at2; -.
DR   Proteomes; UP000002222; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00088; HPT; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd01007; PBP2_BvgS_HisK_like; 4.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 8.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   Pfam; PF00497; SBP_bac_3; 4.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00062; PBPb; 4.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 4.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002222};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1059..1110
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1111..1165
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1249..1300
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1318..1539
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1557..1679
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1707..1821
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1860..1960
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         1611
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1756
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1899
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   2035 AA;  231798 MW;  409CDEA24054FFA8 CRC64;
     MKWLWIVLCV PFFLFGQEAL VLSHQEKVWL NGQKEIYIGA MDDWAPINFV DYHGKASGIG
     SEIVAELNKL LKGKLKIVSG SWEEIYTQAK EGKIDAIMDI TKKPEREAFF YFTKAYLNIP
     HVIVSRQDTP SFGSLESLYG KKVALEKNVG TIGYLRTNFP FIEIQTYDTT SMALHALAMK
     EVDAYIGNRA VMSYKIEQEF LNSLKIDALE RSRKSVPLSL GVPRSNPMLF SILEKSMEAI
     PRETWVKILS KWSNEKPLSL DLTSEERAYL KMKKELRFVA GNEEWKPFSF LDKNGQMQGL
     EKDFLKLLES YLSVPIYVTH LPWEDALKQA KSHHFDGIIS ASPTPDRLEK LSFSHAYYIS
     PLAVVTRHDN VRDINENFAQ KRIAVMEGSA VVLHVKEHFP EAKIVYTKEG TQGLITMLLK
     REAEGAIDTM LSLEYLLKEK SLDAQVEIGY SFYSEALSSF QYALRKDEPL LLSIINKAID
     AYSLDERKNI KERWESKNGN GMKTVSLKGE QKPLTTLSKE EIQWIKEHPI IKVSNEPDFP
     PFDFMKEGRA VGLGVDYMNF VAQKVGLHVS YVQSTWEDLL KQFEAGKMDV LQSVYLTKKR
     QEYAYFTTPF FTNYPAMAVR KGSSIKSLAE LKGKKVALMR GYGTSEKLLR DIPEIKPIMC
     TNVYEALHLV SFGEADVAFD SVGTMSYAIM EQMLTNLSIH KIDVSDKELS SDVHFAVKKE
     KAILYSILQK ALDAMTPEEH IALRSKWVFS NETNFQAEQK SHFQLSSQEK AWLKEHPILL
     FTGDPRYLPY EAFNKEGKYI GIVADLLQKM EKELGIHIEK VPSLTWQDAL LKAKNKEVDM
     ISAYENDKIL SETHLSTKPY VSSPLVIVTR KDKHKYFLNS LLELENQKIA IIKDYSYIQG
     LKAAYPKLHY MEVENAKKGF EGVASGEYDA MVVSLRLATY ALHTMGLHNL HVIGKTDMNM
     HLAFNVKKEW EPLVGILNKA IAAIPPEELQ QILKRWGPED IDTPFDMTLF LEVVSFALLA
     LIALFYWNYL LKRQVASKTA ELSSLLKSFD AHVIASKTDL KGVITYVSDA FCQISGYKRE
     ELMGKNHRIS RHPDNDAKIY EEMWAVITHG GAWKGRIKNK TKEGGYYWVD SVIEQELDAS
     GKVVGYAAIR HDVTAHVELE ELSEKLESIV EKRTQDLAFL NKEQQAIFDS TSVGIVLLKE
     RLIVQCNKRI DEMLGYKIGE QLNQSTDIWY REIPDYQSVY EQVWHGEVVR FEHRLMRKDG
     TLFWARLSGR AIDYLDKEKG VVVVVEDIST EKEALEAIQR AKSLAEEATQ VKSAFLANMS
     HEIRTPMNAI IGMAHLALQT ELSNQQRNYL VKIDSASKHL LGIINDILDF SKIEAGKMRF
     ESIDFYLEDV MEHLADLSVM KAQEKGLELL FDIETNIPTA LRGDPLRLGQ ILINLVNNAI
     KFTAQGEIRL FVKLLAQEAK QVHLLFEVHD TGIGIDEAQQ AKLFEAFSQA DLSTTREFGG
     SGLGLAICKH LVEMMQGKIW VKSTLGEGST FSFSAQFELQ EEQKKPQFND EDVRNLRILI
     VDDNASAREI LENILRSFHF NVHSVCDGHH ALSLLKEAQK EPQPYNLVLI DWMMPQLNGI
     ETIRKIREEI VSDQPLMFIM ITAYSKEELQ KELEELFVDG ILIKPISPST LLNTILNVLG
     KEVMRLSRKE DKQALYRESI HALRGAKVLL VEDNIINQEI AKEILEREGM DIVVANHGKE
     ALEWIEKESF DGVLMDCQMP VMDGFEATRL MREGGHTLPI LAMTANAMEG DKERCLACGM
     NDHISKPIDM AKLFITMAKW IVPSNPRPLK IIQKEERADR PLLNVEGLDI EKALLHVNNN
     HALLETLWRR FVETQAECAE RIEEALRIGD TEKAMREAHT LKGLSGNIGA RELFESSKNL
     EHSLKESSSD IPLFLCQTKQ DLETVIAHLK EAFLDEATHK EVLDFEAILT QEALHEKLND
     LGYLLKELDS EAIDVLANIR ASLFHLGYKK EVEEMEKALA SFDFEKAYAL LKEIK
//
DBGET integrated database retrieval system