ID A0A1H2SSI2_9RHOB Unreviewed; 820 AA.
AC A0A1H2SSI2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444336_101759 {ECO:0000313|EMBL:SDW34621.1};
OS Albimonas donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=356660 {ECO:0000313|EMBL:SDW34621.1, ECO:0000313|Proteomes:UP000199118};
RN [1] {ECO:0000313|EMBL:SDW34621.1, ECO:0000313|Proteomes:UP000199118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17890 {ECO:0000313|EMBL:SDW34621.1,
RC ECO:0000313|Proteomes:UP000199118};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FNMZ01000001; SDW34621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2SSI2; -.
DR STRING; 356660.SAMN05444336_101759; -.
DR Proteomes; UP000199118; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDW34621.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199118};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 308..361
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 373..429
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 498..705
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 696..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 88737 MW; B751307AC3E7ED2E CRC64;
MKGGWSRAAR LQVTVLVVLV GPVLAALTGW ALSGGVDGPV RQETLRGVFL LDVVYILVIA
GLVIWRVTAL ISARRARSAG SRLHLRLTGV FAVMALAPTI LVAVFATLTV SFGIEGWFSD
QIGSVVRNSL VTAQSYEQEH RRRIRAEILA MANDLNRAGE QGINDGQLGE LLRAQARLRE
FPEAYVFDSS MELRARGEFS YLFGFVPPDT EALARARAGE VVVVSDSDAN EIRALVYLRS
FFDYYLLVSR NVDGEVLRLL DETQDTVQLY ERLEKDRSTI LLEFAILYVG FALVVTLAAI
WAGLYFAERL ARPIGRLAGA AERVGAGDLD VRVREERGDD EIAVLSRIFN RMTEQVKGQR
DALVAVNHET ERRRRFMATV LGGVTAGVAR LDAAGRVELL NEAGARMLGV TPLEAAGRPL
GELAPMFQPL LDQARDRRAG HATDRIHASL QGADRDFLAR VARTAPDGDA EAFVLTFDDL
TELVAAQRMA AWGDIARRIA HEIKNPLTPI QLSAERLKAK FAGRLEGRER ERFDSYSDMI
VRQAGDIRRM VDEFSRFARM PAPVPEPNDV GEILREAVLL QSEAGGSVIF EAVEHGEPRA
IRCDRGMLAQ ALTNLLKNAG EAVEARLALR PEPPGRVRVE LTRTPEAEVI RIMDNGVGLP
ETGRSRLLEP YVTTRDKGTG LGLAIVKKIV EEHGGGFALD DAPEGWDRPD GADATPGDAP
QDESEPARQG DEKHAPRGEA KNAPRGAMAV IRLPATPAGG GKGPGTGTPE GGGPSTARAG
TDNNANREAD RRKAAAQTAE TETGRADLAD GGEAGAGTHG
//