ID F8E4F0_FLESM Unreviewed; 2009 AA.
AC F8E4F0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Flexsi_0766 {ECO:0000313|EMBL:AEI14436.1};
OS Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Flexistipitaceae; Flexistipes.
OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI14436.1, ECO:0000313|Proteomes:UP000006621};
RN [1] {ECO:0000313|EMBL:AEI14436.1, ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX PubMed=22180813; DOI=10.4056/sigs.2235024;
RA Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Genome sequence of the moderately thermophilic halophile Flexistipes
RT sinusarabici strain (MAS10).";
RL Stand. Genomic Sci. 5:86-96(2011).
RN [2] {ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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; CP002858; AEI14436.1; -; Genomic_DNA.
DR RefSeq; WP_013885934.1; NC_015672.1.
DR STRING; 717231.Flexsi_0766; -.
DR KEGG; fsi:Flexsi_0766; -.
DR eggNOG; COG0715; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_233754_0_0_0; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000006621; Chromosome.
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; cd00130; PAS; 3.
DR CDD; cd13553; PBP2_NrtA_CpmA_like; 1.
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; 4.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR044527; NrtA/CpmA_ABC-bd_dom.
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; 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 NCBIfam; TIGR00229; sensory_box; 3.
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; PF13379; NMT1_2; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 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; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AEI14436.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006621};
KW Transferase {ECO:0000313|EMBL:AEI14436.1}.
FT DOMAIN 241..275
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 368..428
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 441..491
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 492..558
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 563..615
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 616..691
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 695..746
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1288..1512
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1531..1657
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1679..1799
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1838..1934
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 737..778
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1233..1281
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1585
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1728
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1877
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2009 AA; 225396 MW; 5BFFA12D53B9F317 CRC64;
MMSKGKLSFT DLQFDKKWEY HSADGKASYI SGIIPGHLLY SKLSGNAAEY MVDEIVPFLE
AAYRDGGFTG TEFIRFADYS GVNEASLNAR RAYGRAINQL NEKYHCHPCV TYIIGANFKM
RTLLKFFGKF MKQDYIFVDN IEDAFEHLNS TENRKVSDLP PDEENMENDN LTITPKHISE
LTSALGYILW ERESITSDDW KRFFSEDNPL RSVEDLLSVT ADDITELRQN EKKRTEELSE
SLSLIEATLE STADGILVVD TEGKVLRYNN RFAKMWRIDK DVLATGRDED LLNAVLGYFD
DPEAFLAGVR SLYATPEQTS TDELCLNDGR IFERYSCPQW HDGEVTGRVW SFRDVTEQRK
AEDALRESEE KFRNLAQTTS TAIMVHQNDK WVYANPAAVE IGGYSSEELK TMNFWDLVAP
EFKEKVKERG KKRERGIEVI SEYESKIITK QGEERWVQLE ATSTEYKGEP AVLVSATDIT
NRKEAEKELE EREEYYRSIF QQFQDLYYRT DMDGTLVELS PSVQPLAGYE REELIGKPVK
TVYANLEDRE DLLRELREKG SVEDYELTLQ RKNGEKVVAS TNSHIVFGEN GEPVGVEGTL
RDITERKQAE EELKESEQRL DSLISNTPAV IFSYKFIDGE QKITYINDNI QNVLGFEPDD
FIGNEEFHQS CIHPDDREES FKEIQKLIQG KADSITMTYR FKDSSGDYHW LRDTHRVISR
EDNEIEIVGA WWDISERKQA EQEFQRLLAE SERVNRLMSG RETRIRELKQ EVNTLAEELG
RKRVYADEDE DSAARVEIVE ERAAEPLSAP EPLTGQAYEI ADRGLEKPEV SMAFIPILCC
APLLYAKTHG IFAKNGLEVA LSPAPGWSGV KDLLSFGHCD AAHLLSPMPL AIRQGLDGRP
APIRLASIQN VNGQALTLAS RHKEIADVRE MKGFTFGVPY HFSMHYYLLC LFLAEHGLDP
LRDVSIIEVP PPRMPHFLAT NRVDGVFAPE PFNQLPAYQG TGFIHTLSRD IWPGHPCCCF
ASTEDFIEKY PRTYRVMLKS VMEAELYLHQ AGPEEMQKVA RELSQPDILG QDDPEPVAQA
LSGEYDDGLG NQRIVHDRMD FLPTPWQEYG VWILSQQQRW GQLRRQVDYR EVVEQCFEKE
TRDIAAAMGF DEPGASLEPV APFDGTNAFA YMSAQPFCAF AQEEPAPADS MEERIAHLSR
IVSAKAGGRD PEEIRVQADD VLGWLEQCIH DLIKNLDFAA DALTESKETL EQEVQKQTAK
LEEARKNALS LAEDAEAANK SKSEFLANMS HEIRTPLNAV MGMGQLLADT PLNDQQRNYL
AKIDRSSKLL LGIINDVLDV SKIEAGKLEL DPHSFNLHDV VNDMRTMFSS KAQKKRLELI
IEADPDLPRA LVGDSMRLEQ VIANLLSNAL KFTESGHVSL HINKAREAAT SPDSCRLRFS
VTDSGIGMNE EQMGRLFNPF SQADSSTTRK YGGTGLGLVI SRRLVEAMGG RLEVTSAPGE
GSTFFFTIEL PKASDQTGLA DRPASLSDNM KFLVVDDQEP ARIVLREILE SWNGDVVEAA
GGRKAVEEVL AAQKQNRPFD FILMDWKMPG EMDGLEAIRH LKHLHETGTL TGDETPVFMI
SAYSEDEIPR SESDLYQAFL EKPVTASELF DAIMQATGKE MGTVQQTNSA TTPSFAGYTV
LLVEDNEMNQ EVATAFIEKT KAKVITAENG TDALQCYEEN SIDLVLMDLQ MPVMDGFDAT
AEIRRRENDS EGNAHVPIIA LSAAVLDADR KKAAEAGADG HLGKPIDSQE LYAVMGQYLK
SSGSISEESA SPEEEAAEEF PVLEGFDLSR GKASAQGKRD TYLKLLRNFY TQITGAFADF
PDRISSLTFE EIHHEAHTIK GVAATVGALR VADAAAAIDM AGIEQTAPTE SMINELRDAL
LCAKEQIAPH LSIEKSTVAV GEEEGRKAMD TLLEILRNNE LPEDDLVETV VAFVGAEAGS
EKAGALRSSI EQFDMDSAVD LLEKFQQGE
//
