ID A0A286GI25_9PROT Unreviewed; 1111 AA.
AC A0A286GI25;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421508_104246 {ECO:0000313|EMBL:SOD95160.1};
OS Caenispirillum bisanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD95160.1, ECO:0000313|Proteomes:UP000219621};
RN [1] {ECO:0000313|EMBL:SOD95160.1, ECO:0000313|Proteomes:UP000219621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 140 {ECO:0000313|EMBL:SOD95160.1,
RC ECO:0000313|Proteomes:UP000219621};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; OCNJ01000004; SOD95160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GI25; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000219621; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
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 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; 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; 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; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000219621};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..308
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 381..431
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 432..499
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 572..794
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 815..933
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1008..1101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 941..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 864
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1047
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1111 AA; 118587 MW; E5486F029D78E20D CRC64;
MTRRSDAILL AAAATAVGGI LAAASAPLTG AAAGPAGGAV ALAAAGWLAV EAVRCKRRMR
VQTRLLDGTA DAVVAVTPAR VVVAANRAAR DLFGEEPPLT GRLLEDIVPG AGEAATLATL
GTERNGVREC TGRALDGSDV PLEVTARTLH DGITILAFRD ASQRHLADAA LRRKLRELEN
NTRLLREIET LARIGCYDFY PGADEALWSR ELERIFGLEG DPANPIRSFD AFLARVHPDD
LPLILADAED QTWREKERMF RIVRLDGEVR HIFSKGYREF GPDGRVVRLF GIDQDVTDRV
AAEAALRDSE ETLRRVFDSA PVPLVLVDQA SGRPLAANRG ARQLFEVGEE ELGGLRSTDF
YDDPADRDRL MATIAREGGV AGWELRLRTR KGRTLWLETS GTLISYQGRP AFLGGFVDID
ARKQAAAALR DSEDRLRSLL ARLPLPLSVV RLSDGRILFC NDLAAVYLGV SPADAVGLGA
VGFFVDRQEF DRVMGALRRD RCLRDMEFRL PDGPDGARWG VASAVALEYE GEDAAVSVGI
EITDRRRAEE ILARAKVDAE TLARAKSEFM AVMSHEIRTP MSGILGMVQL LAGTRLTKTQ
ASYVDTIQRA GDTLLRLMGD ILDVGRIEAG TLALAEADFA PRDLLDRIAT LMRPWALSKR
LELSVEVADG IPPLLRGDEG RINQLLFHLV SNALKVTERG GVRLRMRPLG AAPAGGLRVQ
IAVDDSGPGI PEDQRDRLFE RFAVADASAA RQHGGAGLGL ALCKGLVTAM GGRIGFDTMP
GRGSTFWVTL DLGEGEAPAD ANGGVAAEAP PGGLRVLLVE DDKVNRMLAV ELLRRAGHRV
KAAADGLDGV AAAAEGVFDL VLMDLHMPGI DGAEAIRRIR ALPDTARATV PIVVLTADIT
EEGRTAAREA GADTVIAKPF RIDVVNRVVA DLLGRPLPLV PPRATADAVA GPSLPREPAP
PPRAAPPRAP APPVPAPAPA ADRPALPPLD PRLVPSDSLI VRQWDDLGPE AVRGLVELFR
TTTPPRMETL DAAITGGDAA TVVDEAHALK GAAGVLGLTP LHRLYQEVEG DALAGDLDAV
AQTMPALRRT YDETLRALAA FDAAPAADGV S
//
