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Database: UniProt
Entry: A0A1T4JZJ4_9BACT
LinkDB: A0A1T4JZJ4_9BACT
Original site: A0A1T4JZJ4_9BACT 
ID   A0A1T4JZJ4_9BACT        Unreviewed;      1129 AA.
AC   A0A1T4JZJ4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04488132_101339 {ECO:0000313|EMBL:SJZ35544.1};
OS   Sediminibacterium ginsengisoli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Sediminibacterium.
OX   NCBI_TaxID=413434 {ECO:0000313|EMBL:SJZ35544.1, ECO:0000313|Proteomes:UP000190888};
RN   [1] {ECO:0000313|EMBL:SJZ35544.1, ECO:0000313|Proteomes:UP000190888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22335 {ECO:0000313|EMBL:SJZ35544.1,
RC   ECO:0000313|Proteomes:UP000190888};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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};
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DR   EMBL; FUWH01000001; SJZ35544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4JZJ4; -.
DR   STRING; 413434.SAMN04488132_101339; -.
DR   OrthoDB; 9811889at2; -.
DR   Proteomes; UP000190888; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SJZ35544.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000190888};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          477..701
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          746..858
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1010..1127
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          391..456
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         795
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1060
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1129 AA;  127044 MW;  79915984EBE358F3 CRC64;
     MIRSLPFKLY AGLVIAVLLV LIVGFVSVNA LEKQEEEAEL VRSSNQVITS IRQLRFELMR
     VRSARRSYWV TGNESYLDQF QKGAVAIPMS VSSLKQLVID DAAQTNHIQK LDEIFAEIFH
     YWQKEGRITP EMDKAAFARV VNTEEQMLKN AINQFDTARI TEERQLHARE RSARKHHVET
     RTILFTGIGI LMVVVLLLIN SVLQTLKSRY KSGLKLKESL AEMEKINKSA QEKNWVLEGM
     SYVNNRMQLV DSTRELAGKI IDALVQYLEL PAGVIYFYDE KEQKLFTVAS VSVSSSASKE
     YRIGDGIVGN AALSKTPVLI KHIPPDYWKV ESMLGQVTGN GEIICIPLWM NGKLKGLIEL
     GCFESFSSIQ LALLNSITDI LSVAINSYQS RERIDILLEE LQDQQEELRQ INDELSRQTE
     ELQASEEELK TQEAELKQIN LDLKERNETI ESARSALAIK AKELESASLY KSEFLANMSH
     ELRTPLNSVL ILAKLLADNT TGNLTEKQIE YAKIIRKSGK DLLDLINDIL DLSKIEAGKV
     ELDIQPVRIT EIQADIRQLF SVVAAEKGIE FKTEIAADVP ELINTDKQRV EQVIKNLLAN
     AFKFTQKNGT VTLSMSNKNQ FNEPVLSISV SDTGIGISQE KQQLIFDAFQ QADGSTSRKY
     GGTGLGLSIS KELVRLLNGS IDVFSTEGKG STFTILLPYR ISNAKTEKSK SLALSPTAVP
     ELDASKVTLQ QQVEDDRDNL EEGDRPILII EDDVNFATII KDFTRHKGYK AIVAMQGDEG
     LLYAQQYIPA AIILDMQLPV MDGWTLLKKF KADEKLKNIP VHIISAFDDN RLKHADVLAY
     LKKPVDTEEL DKVFTVIEAH LRSGSKKMLL ITDSQFSDTE LTRLFREKKY EIEVEQVAAL
     SQAKKAKENV YDCIIIPVGV DTDKQQLEAV CSEIQSAKIP LVLYLDEGIS GEEEQELKKM
     RSDAMLRSST GAKRLTEELE LFLYKMKEVV RQPETIYPEM VNDTSLENKK ILLVDDDMRN
     VFAISAALQA NGMEVVAASD GKEAIEQLKR YSGIDLVLMD IMMPEMDGYE AMQKIRNEMK
     LIDIPIIALT AKAMAGDREK CIAAGASDYI TKPVDMQKLY SLMRVWLTK
//
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