ID A0A1F8PCQ8_9CHLR Unreviewed; 1168 AA.
AC A0A1F8PCQ8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2Z15_00700 {ECO:0000313|EMBL:OGO20933.1};
OS Chloroflexi bacterium RBG_16_50_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797642 {ECO:0000313|EMBL:OGO20933.1, ECO:0000313|Proteomes:UP000179337};
RN [1] {ECO:0000313|EMBL:OGO20933.1, ECO:0000313|Proteomes:UP000179337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO20933.1}.
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DR EMBL; MGNJ01000002; OGO20933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8PCQ8; -.
DR Proteomes; UP000179337; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 66..118
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 119..190
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 266..293
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 318..368
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 369..439
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 439..494
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 495..564
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 807..1023
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1043..1163
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 478..505
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1097
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1168 AA; 130645 MW; 5A25C3D6768249F3 CRC64;
MAKIGSYEYD PVTGISIWSS EMFNLVGRDP ALGPMSVPEF MQLMHPEDRT AMQSMLEGCA
RDGVSGAIEF RGDPASGEIR YFIGNVQAAS DSKGRITKLF GTIQDITERK QAEEALIASE
IRYRRLFESA KDGILILNAE TGQIVDVNPF LFNLIGFSFE ELMGRKLWEI GLFKDIAASK
EAFKELQDKG YVRYEDLPLE TKDGKKRDVE FVSNVYQVSN MRVVQCNVRD ITERKRAQDT
IKESEERFAT AFRNSPILMA ISTLKDGRFI ETNDAFCRAM GYRHEELLGH SSLELNLWYD
PGERMATLEK MKGREELSNL EVRFRTKSGE TRTAEMSMVK IILRNEPCLL IIAMDITERK
LLEEELEREY EENKLIIDSS PVLIFYKDRE GRFLRVNNAF AVALDMPEDK FLGRTVFDLY
SADIAQSMTN DDNEVFESGI SKLSIIEQYE SARGIRWVQT DKVPILDKSG KTIGLVGFAQ
DITERKQAEE AIRESEEKFN KAFHASPNLM AVITLDEGRI IDVNEAYSTI TGYKREELWG
NVALELNLWA NPEQRKDFYQ KINKDGRLDN MEILLRTKAG EIRAFLFSAE KITLRGIPCL
VTVALDITER KLAEERINHL NLTLQSVRNV NQLITREKDR DKLLKGVCDT LVKGRSFFTA
WIVLLNESKE VITHAASGIR GDFTPLLSRI KQEETLPCIQ KALKKSGVVI TENPHTMCAD
CPAIANSTDF GSMTVRLEYE GAIYGILCSS LPKSILTDKS EAELFQEVAT DIAFALHNME
MESEYTRLEQ ERLRVAKLES IGTLAGGIAH DFNNLLTGIM GNIGLVKTYI APSDATYEML
NEAENAAARA RDLTQQLLTF ARGGKPVKKL TSVAGVIKES AEFALRGSKV KLELSLPDNL
WPIEADEGQI NQVINNLAIN ADEAMPRGGT LKIRAENLVY KKSAALPLQS GNYVRVDIED
TGIGISPENL QRIFEPYFTT KQRGSGLGLT TAYSIVRNHN GIILADSILN RGSTFRIYLP
ATKKILKGGK KVTVESAGQA GGKVLVMDDE EIIRKMLKNM LSLAGYTVEL AADGDEAITK
YQQARAAGDP FNAVIMDLTI PGGMGGKEAV KKLLEIDPKA TVIVSSGYAT DAIMSEYKKY
GFKSVIAKPY SVRQLQDTLS GLLTKKKR
//
