ID A0A0J1B6Y8_RHOIS Unreviewed; 861 AA.
AC A0A0J1B6Y8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RISK_005563 {ECO:0000313|EMBL:KLU02497.1};
OS Rhodopirellula islandica.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=595434 {ECO:0000313|EMBL:KLU02497.1, ECO:0000313|Proteomes:UP000036367};
RN [1] {ECO:0000313|EMBL:KLU02497.1, ECO:0000313|Proteomes:UP000036367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24040 / K833 {ECO:0000313|Proteomes:UP000036367};
RA Kizina J., Richter M., Glockner F.O., Harder J.;
RT "Permanent draft genome of Rhodopirellula islandicus K833.";
RL Submitted (MAY-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLU02497.1}.
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DR EMBL; LECT01000044; KLU02497.1; -; Genomic_DNA.
DR RefSeq; WP_047816533.1; NZ_LECT01000044.1.
DR AlphaFoldDB; A0A0J1B6Y8; -.
DR STRING; 595434.RISK_005563; -.
DR PATRIC; fig|595434.4.peg.5282; -.
DR OrthoDB; 9762493at2; -.
DR Proteomes; UP000036367; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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 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; 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 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; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 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 Kinase {ECO:0000313|EMBL:KLU02497.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KLU02497.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..555
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 585..703
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 748..846
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 707..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 634
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 787
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 861 AA; 95082 MW; 33A54267EBEE6A1D CRC64;
MWQAWYEFRI DYVLFSVVFL AGHAFILSRV RRAMPPASST HPDSATSPAA IGSSRRPRLS
FWILLLLLTG GFLAVETADR LQRSRLRQQV FGIAPTYAAE LQQLGHAGIN KETSPDDPVY
RRMINAQKRW LSVNPQVTDI YTMRHLSESE LATHLLTEQD RPTGQPFQII VDSETDYNGD
GKIEGVREGQ TEIGEIFYDS SVEQIERAFR GDTTFADQPS HDRWGEWVSA YAPLFDSKGK
VEALVGVDFP AKHYIHSVIL TRLGVIGMIA ALITLFLGAV TSIGMLKAGI AAQQRSHALL
QDQRDLATQA ASQARQAAVT KNQFLANMSH EIRTPMHGIL GTTELMTRCS LNEEQRHYMH
MIQTSAKGLL TVLNDILDFS KIDSGLMTLE SVPFELKDLL SQTMHAVANL KNENVQLQFQ
PPVGVPEIIV GDPTRLRQVL INLVGNALKF TEQGRVTVFI EKESQDATIL DTSEDQSSRI
VFTITDTGIG MTEQQRANIF EAFTQGDSST TRRFGGTGLG LSISSQLVEL MGGQLQVSSV
LDEGSSFRFD IPLRTPIGTT QHEIEKLHPP SAPTNSFGHC AQTRELLLVE DGAINRTVAE
TMLRARGHRV TSVSNAKDAL KHLRSQAFDL VLMDVQMPEI DGLTATQIIR NDLPSPARDI
PVIALTAHAM REDRQRCLDA GMNECLTKPY PPELLFDTIE SFTISRQDDQ DDLLLPPTTS
RTTSSPSSPV DRASPLNHEV ILQNVGGDLQ VLTMLAQTIS DELPSQIEQL QRAIHAGAWT
QVARAAHTLK GTAAAIGATQ AQEIADSMET FCLGETSEEE RSHFLENRMN ALVSAFELAQ
TELKKFLRSS SGSDHPGNET P
//
