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Database: UniProt
Entry: A0A099PCC1_9GAMM
LinkDB: A0A099PCC1_9GAMM
Original site: A0A099PCC1_9GAMM 
ID   A0A099PCC1_9GAMM        Unreviewed;       604 AA.
AC   A0A099PCC1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   03-MAY-2023, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=LH51_11170 {ECO:0000313|EMBL:KGK41912.1};
OS   Nitrincola sp. A-D6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK41912.1, ECO:0000313|Proteomes:UP000029924};
RN   [1] {ECO:0000313|EMBL:KGK41912.1, ECO:0000313|Proteomes:UP000029924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-D6 {ECO:0000313|EMBL:KGK41912.1,
RC   ECO:0000313|Proteomes:UP000029924};
RA   Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA   Fernandez S., Ferrer A., Chavez R., Levican G.;
RT   "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT   Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL   Submitted (SEP-2014) 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   -!- 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:KGK41912.1}.
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DR   EMBL; JRLB01000061; KGK41912.1; -; Genomic_DNA.
DR   RefSeq; WP_036522185.1; NZ_JRLB01000061.1.
DR   AlphaFoldDB; A0A099PCC1; -.
DR   STRING; 1545442.LH51_11170; -.
DR   OrthoDB; 1931120at2; -.
DR   Proteomes; UP000029924; 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; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; 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; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12974; Phosphonate-bd; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029924};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        313..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          379..600
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   604 AA;  68363 MW;  2DCF626B83DF8F16 CRC64;
     MILAKKVRSS LLFILLLCII CSEVAAEEIH IGILDWRTLE DFEQHWLPSL QSLEKEMPAH
     RIVLHPMTLN ELNKGVADNQ LDFLITNPGH YVALSSEYRV APLAQLQHLK AGLPLNHVGS
     VVLTHQGRQD LNEFTDLKGL TIGAVSPESF GGYQLMLDTL HLRYSDIKSW DIHWNFTGFP
     MDQLVEKLLN DEFDAIVLRS CLAEVLALEG SVDLSSLRLI GTQAIDTYPC MISSAVYPGW
     PLLRTAKVND TLARQVLAAL MKSDSILIDQ DVMYWQPPVS YQSVYEVFER LRIGPFAAFP
     HNPIMHWLIM HRHWFYGAFA LLILLVLHNI RAEYLVRKRT QELEWSQQCQ REAEQIALHH
     QDELRHASRF TLMGELAAGL AHELNQPLTA IANYARGSVR HLQRQDQDLL ARRTQLVEAS
     EQIANQADQA AAVIRNIRTF LKKDTGEYNW LAIVPLVENA LLFCQTRIKQ AQIKPQLQCD
     DHLPDIFSHR IHLLQILANL ITNALDAMVD VDVDQRELCL SIHQDKANNR LIIQVADRGK
     GIDAAIEKHL FEPFMTTRKE GMGLGLSLSR SLAEALGGQL ILKNRSTGGA MAELTLPIQP
     LLQE
//
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