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Database: UniProt
Entry: A0A1H2SSI2_9RHOB
LinkDB: A0A1H2SSI2_9RHOB
Original site: A0A1H2SSI2_9RHOB 
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}.
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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
//
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