ID A3K718_9RHOB Unreviewed; 886 AA.
AC A3K718;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SSE37_13146 {ECO:0000313|EMBL:EBA07145.1};
OS Sagittula stellata E-37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sagittula.
OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA07145.1, ECO:0000313|Proteomes:UP000005713};
RN [1] {ECO:0000313|EMBL:EBA07145.1, ECO:0000313|Proteomes:UP000005713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-37 {ECO:0000313|EMBL:EBA07145.1,
RC ECO:0000313|Proteomes:UP000005713};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:EBA07145.1}.
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DR EMBL; AAYA01000011; EBA07145.1; -; Genomic_DNA.
DR RefSeq; WP_005861344.1; NZ_AAYA01000011.1.
DR AlphaFoldDB; A3K718; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000005713; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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 Gene3D; 3.30.450.20; PAS 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
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 Kinase {ECO:0000313|EMBL:EBA07145.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005713};
KW Transferase {ECO:0000313|EMBL:EBA07145.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 224..295
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 303..353
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 371..589
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 614..731
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 735..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 663
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 886 AA; 95839 MW; 6BA18E7F1D587C96 CRC64;
MTSHRTSFSI SRSTLVRRIL AASVIAVLMA VIVVLGLEVP RQLARLDESA AENVQWTIGQ
AETEVIALEL AAAHAISDPD DPAGLDEVRL RFDIAYSRIE TLQRAKVLEE LRSGDEVDNE
LTAAVDFRDK WVSVIDSPDD VLRAALPDLL DAAQEVRTDL RRLALSGIAF FARVGDMRRE
EIINTLFSIG LMTIALVGIL LILISAVLRL ARQREGEAQA NFETRRRMET IISTSLDAVV
AVSRENRIIE WNGAAERVFG YTRAEAIGTD MPTLIVPPHF REMHRSGMSR YLNDGEPRVI
GRGIVQLEAM RKDGTVFPVD LSLAKANSPT GEIFVAFLRD ISDRVRSDEA LRRARDRAVA
GEKQKAELLA VMSHEMRTPL NGILGTLELL EADSLPAEDQ RYLRIIRQSS EILLGHVNEV
LDISRLDAGK MTLRKTRFDL VALLEEIVES QADRARAQGN LLTLRPPNPA LHEVYSDPDR
LRQILLNLVS NAIKFTAGGR IMIEADCDSG MDDCELRVID TGVGIKPDDL ARIFDDFVTI
DSSYGRRNTG TGLGLSISQR LATALGGELG AESEPGDGSV FWLRLPLAPP VGAPVARPRA
ANAPAPAPVL PPLDVLLVED NAINREVARH MLQRDGHKVT EAHDGREGVE AAQTRDFDVI
LMDISMPGMD GIQASRAIRQ SGGHSVATPI IATTAHAMPE EVRAFHAAGI ATVLTKPISA
NALRQSLASV LAPERLPEAP PPAAPHETPA NSAPSAGTHA ALIDLAHLDE VREDLPEDKL
AAALHTFACE LEDFMSSLSV DEFAGTDAAE TAKLGAEAHR LAGSSGVFGA LPLADALRAF
ERHARADDKT ALASDAAALQ TTWRETRAAL RAEGLDTAAP APGAPT
//
