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Database: UniProt
Entry: A0A1I0G9S3_9CLOT
LinkDB: A0A1I0G9S3_9CLOT
Original site: A0A1I0G9S3_9CLOT 
ID   A0A1I0G9S3_9CLOT        Unreviewed;       577 AA.
AC   A0A1I0G9S3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05660297_03109 {ECO:0000313|EMBL:SET67504.1};
OS   Natronincola peptidivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Natronincola.
OX   NCBI_TaxID=426128 {ECO:0000313|EMBL:SET67504.1, ECO:0000313|Proteomes:UP000199568};
RN   [1] {ECO:0000313|EMBL:SET67504.1, ECO:0000313|Proteomes:UP000199568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18979 {ECO:0000313|EMBL:SET67504.1,
RC   ECO:0000313|Proteomes:UP000199568};
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; FOHU01000019; SET67504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0G9S3; -.
DR   STRING; 426128.SAMN05660297_03109; -.
DR   Proteomes; UP000199568; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 1.10.1760.20; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:SET67504.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199568};
KW   Transferase {ECO:0000313|EMBL:SET67504.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          227..362
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   577 AA;  63988 MW;  FDA9DA5F024AF8B8 CRC64;
     MILIIGEMML SLLNKLGIII ILAVIISKIG IFRKLIIKKN ITFMDKIFLS IVFGAIGIMG
     TYSSVPINGA LANTRIVGVM VGALLGGPMV GFMAGLIAGG HRFLIDIGGF TAVACGVATI
     VEGLFGGYAH YYIRNKSPKW EWAFLLGVIS EFIQMIIILL IARPFGDALQ LVKIILFPMV
     VVNSFGIAIF IGIIENIYTE YDRIAASQAE KTLKIANLTL PYLRQGLNYE VAQKVVGIIK
     ESVDVAAVTI TNRHEILAHK GIGEDHHCQG FDLQTEATKE VIQTGQYKII NDKDSIKCIK
     NDCTLKSAIV VPLKERDRVV GILKLYRTEE NSITSIDTEL ALGLAQLFST QIELSRVEHQ
     NKLITEAELK SLQAQINPHF LFNAINTIVS FIQFDSGKAK QLLISLAELF RKSLSNNQDM
     VDMDVELKHI ASYLEIEKAR FGDKLQVKYD IQKNVVCKLP PLILQPIVEN AVVHGILPKK
     SGGSVTIRCR KNHEDILLEV IDDGIGMEAE ELKGLLNQQS DTNCIGLMNV NRRLINLYGE
     EYKLQIKSTY NEGTSVLIKI PYVKGRYSSE VKEEIVA
//
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