ID A0A2Z3H227_9BACT Unreviewed; 1032 AA.
AC A0A2Z3H227;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-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=C1280_16270 {ECO:0000313|EMBL:AWM38392.1};
OS Gemmata obscuriglobus.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Gemmata.
OX NCBI_TaxID=114 {ECO:0000313|EMBL:AWM38392.1, ECO:0000313|Proteomes:UP000245802};
RN [1] {ECO:0000313|EMBL:AWM38392.1, ECO:0000313|Proteomes:UP000245802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5831 {ECO:0000313|EMBL:AWM38392.1,
RC ECO:0000313|Proteomes:UP000245802};
RA Franke J., Blomberg W., Selmecki A.;
RT "G. obscuriglobus.";
RL Submitted (JAN-2018) 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; CP025958; AWM38392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3H227; -.
DR KEGG; gog:C1280_16270; -.
DR OrthoDB; 220475at2; -.
DR Proteomes; UP000245802; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 4.
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; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000245802};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..207
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 263..316
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 340..390
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 391..460
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 463..513
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 510..583
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 584..638
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 651..875
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 895..1011
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 946
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1032 AA; 112041 MW; 61E2F78A854D54BE CRC64;
MSRPRTHIQL APPPRVYAVP AAVAAAGAVR FLLDPILGET HPYILFIFPA LYLANRAGWK
SGAVALVLGM MLANFLFAVP RMSFCVAAPE NQVGLLVYLA VGGAGVYLAD ARRTAQGLAE
ASAAAVATES AAHRQTQEAL RKQQARLLDH AFDPILTWEL GGNITYWNAG AERLYGYTAA
EAVGRSAHEL LQTVLPDSRT ALEATLRCGG RWEGELRHRT KGGNWVVVDS RMVVARATGA
LEILQSDRDV TDQQRVEADV RDALERFRGV VEQAVDGIIT IDERGTVETV NPAVARVFGY
APDEVVGRNV SLLMPDPYRG EHDGYLADYL RTGTAKVIGV GREVRGRRKN GTEFPLDLTV
SEIRVASGRR FTGIVRDITE RKRAEEQLRA SEARFRNFVE QAADAFFLHD AGGTILDVNR
RACESLGFTR EELVGMRAEA IDPDLSPDLL RRVAEDLATG RQVSLDARHR RKDGATFPVE
VRLSPFEVDG RRLVLSLVRD ITDRRLAEES LRLRDRAIQA VTQGILITSP ALPDNPITYA
SPGFEGVTGY PPREALGRNC RFLQGKDSDP AAVALVREAV RAGRDCAVEV LNYRKDGTPF
WNALSVSPIR DDAGELTHFV GVLVDVTDRK KLEEQFHHAL KMEAVGRLAG GVAHDFNNLL
TVINGYSEVL LAGMSDESDP DRRAVAAIRD AGERAAALTS QLLAFSRRAV LKPRVLDLNK
VVAETGKLLG RLIGEDVRLS TALDPRAGRV SVDPGQFGQV LMNLAVNARD AMPTGGQLTI
ETRAVVLDEA YAKGWPEVRP GRYVMTAVSD TGCGMTDEVK SRVFEPFFTT KEAGKGTGLG
LATVFGIVKQ SGGHAEVYSE VGVGTTFKVY LPAVSDADAV PLDTAPATVR GGTETVLLVE
DQPDVRRVAL VSLQAHGYRV IEAGDGRTAL DLVERDRPHL DLLVTDVVMP GMNGRQLAEA
LRPLYPGLKV LYMSGYTDDA VVRHGVLQAN VAFLHKPFTP FSLAGKVREL LDQEREPLTG
KDAAAGSAPG PR
//
