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Database: UniProt
Entry: A0A1I2CD71_9BACT
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Original site: A0A1I2CD71_9BACT 
ID   A0A1I2CD71_9BACT        Unreviewed;       803 AA.
AC   A0A1I2CD71;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216283_101700 {ECO:0000313|EMBL:SFE66256.1};
OS   Sunxiuqinia elliptica.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Sunxiuqinia.
OX   NCBI_TaxID=655355 {ECO:0000313|EMBL:SFE66256.1, ECO:0000313|Proteomes:UP000198964};
RN   [1] {ECO:0000313|EMBL:SFE66256.1, ECO:0000313|Proteomes:UP000198964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9156 {ECO:0000313|EMBL:SFE66256.1,
RC   ECO:0000313|Proteomes:UP000198964};
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; FONW01000001; SFE66256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2CD71; -.
DR   STRING; 655355.SAMN05216283_101700; -.
DR   Proteomes; UP000198964; 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   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 3.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198964};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          200..271
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          273..325
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          326..388
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          441..511
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          514..566
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          584..803
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   803 AA;  90330 MW;  C690ED6051AB42F5 CRC64;
     MLQLFIALTQ NAALLVALSV LYSLLSRFRQ QNRTKYSILV GLLFGAIAIA GMNIPVYYEP
     GIIYDARSVI LVLSGLFGGG IASVVAVLMA GAFRLFLGGV GVMTGIITIP ICAIIGLAVR
     KFYHNNPENL SLFKLWTLGF LSHVIMLSLQ LLLPWPTGLD IIMRLWAPIL TIFPIATLIA
     GMLLQTEEKR LNALSKIKST EERFQALSEH SPVGIFRTLP NGYTTYVNPR WSQLSGISKE
     QALGDGWLEA VHPDDRNNLE KRWKEIALNE GRSLAEYRFL RQDGEVISVY GEAVPEFGDE
     GKLLGYIGTL TNITQRKKAE EALRENEQNY RNLFENDPAI KLMVDPDTGQ IINANKAAAK
     FYGWSVEQLV DMKIDQIELT YQTISHPSRG QNGHTQKAKH QLANGEIRTV ELFINQIRFH
     GKDCCHCIIH DITEKQEAEE KLKLLSKALE QSPVSVTIVN PRGKIEYVNP KFTEISGFTP
     DEVIGEKLYK LNPDQFSSEV YKHILQTISS GQDWVGESEN RRKNGERYWE SQIISPIVDT
     NGKITNFISV KEDITEQKRM LKEVLEAKEK AEKAERLKSA FLANMSHEIR TPLNAILGFT
     NMLTSNTNLS QESREEYVFI INKSAEGLLQ IINDILDISK LETGLVKIFK KPFELEQVLE
     SLKARYIKKL AYENKQHINL NLEIAQSVPL LDNDETRFVQ IFTNLLDNAV KFTEEGEITF
     GISNATPERI DFFVSDTGIG ISEKDQANIF ERFRQAGEST ARLQSGNGLG LAIVKNLANL
     MGGNITLQSK QGEGTTFHFW IPR
//
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