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Database: UniProt
Entry: A0A2H3KM45_9CHLR
LinkDB: A0A2H3KM45_9CHLR
Original site: A0A2H3KM45_9CHLR 
ID   A0A2H3KM45_9CHLR        Unreviewed;      1066 AA.
AC   A0A2H3KM45;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A9Q02_15685 {ECO:0000313|EMBL:PDV98395.1};
OS   Candidatus Chloroploca asiatica.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Candidatus Chloroploca.
OX   NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDV98395.1, ECO:0000313|Proteomes:UP000220922};
RN   [1] {ECO:0000313|EMBL:PDV98395.1, ECO:0000313|Proteomes:UP000220922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7-9 {ECO:0000313|EMBL:PDV98395.1,
RC   ECO:0000313|Proteomes:UP000220922};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-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   -!- 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:PDV98395.1}.
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DR   EMBL; LYXE01000102; PDV98395.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3KM45; -.
DR   OrthoDB; 9784397at2; -.
DR   Proteomes; UP000220922; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 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   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; 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:UP000220922};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          327..379
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          563..635
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          637..689
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          702..925
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          948..1065
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         999
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1066 AA;  116646 MW;  7BD39A002B92D6B3 CRC64;
     MSQRTHLSLQ RKLFLAFVLV MLIPIVVLSG YVLVRVRAMI VQQVSTDQLR LLETQATLLN
     GQLVTSGSDL IIALKSAELQ QYVAQHDNPQ SLIQSFATFL RQSQGRYTGL CLLDVAGNEE
     VCVRAAEGAY LPVSELRNRA DAPGFQRTLL QAQANPGLPL TMTRIPFDTN EAPRLDLATT
     YLDDSGAAIG VLVLEMPLEP LFATLHTETP DIEVSVVEYD GTFLFEQNQL TTSTEQVRRL
     DQIHPESAAT ILGQSAGILI KPVDAPGKLL TFARVSPSSR SLLQWTLIYE QPINTLLGGV
     TETYLVIGLI TGLSILVALS AAHLLSMTIV RPIQHLAAAA EQIGAGNLSI PIPQTGPAEI
     RALGQTLDQT VSRLQTALTT AEQRRHEAEA LASAMQMLSA SLNREEVLGL IFSELRKVVP
     YDSASVQAIQ GDTSMIIGCY GLDYAETLIG VRFSLQAGTT PNAQVAHSRT PLILNDAIQS
     YPHFNDDPSI NNPVCAWMGV PMLMGDRLLG IITLDKYEPG FYTVEHARLV AIFATQAAIA
     MEHARLYEEV SRELADRRRA EAAYARLAAI IESTNDLVGM ARPDGEILFL NTAGRHVLGI
     LPNEDLATMR VVDLYPPSRL TWLRTEAIPT VMREGIWSGE SIIYARDGTE IPVEQVILAH
     RTPDGQTEFI STIAHDMRER MRAEEQLRES QKMEALGRLA GGVAHDFNNL LTVIMGEADL
     ILSDPPDDED LRTSITQIRQ SGERAATLTR QLLAFSRRQV LQTETISLNE VLTDIEQLLR
     SLIGERIQLQ ISLDPDLPLV RADPGQMTQV VMNLVINARD AMPDGGMITL TTTQRAITPA
     MEAEYAPVEA GTYAVLTVRD TGQGMDEQTR DHIFEPFFTT KSRGKGTGLG LATVHGIVRQ
     SGGKILFASQ LGQGTQFVIY LPVVATAELP HMASPNPTAQ PRKTKPCTIL LVEDDANVRE
     LTRQLLSRMD MVVLEASDGE AALAIIRSHP TPIDLLLTDV VMPGKLNGFQ LGVAVQKLCP
     TIRTIYMSGY SDTALRQQAL ADQAICYLQK PFTADELARA LHTMVA
//
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