ID H5YM05_9BRAD Unreviewed; 1049 AA.
AC H5YM05;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Bra471DRAFT_04439 {ECO:0000313|EMBL:EHR03654.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR03654.1};
RN [1] {ECO:0000313|EMBL:EHR03654.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR03654.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-2011) 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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CM001442; EHR03654.1; -; Genomic_DNA.
DR RefSeq; WP_007610908.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YM05; -.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000005774; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
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; 1.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
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:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; 3.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 270..332
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 349..421
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 426..478
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 685..908
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 931..1046
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 642..677
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 981
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1049 AA; 113964 MW; 0113A04B642F5AE3 CRC64;
MTTATGVRSA DRNSVLATLG DYIREISNPD DLAYAAAELL GRSLNVSRAG YGTVDTSAET
ITIVRDWNAP GILSLAGVLR FRDYGSYIED LKRGETVICA DAEKDPRVGD RAEALAAISA
RALVNMPISE PDGVVALLYL NNAGPREWSS EELELIRDVA ERTRTAVERR RAETAVRENE
ARLVFLDALN KETARTRDAD GVMAVTTKMV GEHLGVSNCA YADMDPDQDG FTIRGDWAAP
GAMHILGHYS LADFGKKAVR ELGAGRPLII NDNLREIAPD EAATFQNIGI GSTICMPLVK
EGRLTALMAI HHRGPHRWTP RELALLTEVT ERSWAHIERV RSEQAAREAA ERLTLANKAA
GIGTWDYDPV NNVLRWDSRC REVFGLRPDA EVSYEGSFLK GLHPEDRQRA HEAVSAALTP
HAPTTYNMEY RTIGIEDGVE RWIVATGQAI FANGQAVRFI GTVLDITAQK KTERHLRLLN
DTGASVSRER DLDKIVQIVT DAGVGLTGAQ FGAFFYNVLA PDGGSYMLYS LSGAPRSAFE
NFPMPRNTAV FGPTFEGSGV VRSDDILQDP RYGKNAPRKG MPEGHLPVRS YLAVPVISRT
GEVLGGLFFG HAETGKFQAE HEAALLGIAG HAATAIDNAQ LLTRLEALNA GLEQRVADEI
AERMKAEEQL RQSQKMEAVG QLTGGIAHDF NNMLAVILGS LNLAKRRLGR GEVSIDRFIE
GAIDGANRAA TLTQRLLAFS RQQPLAPEIV DINKMVGGMS ELLERSLGEL IRLETVLAAG
LWRVKADPAQ LESAMINLAV NARDAMPKGG RLTIETSNAS IDLMYAREYA LAPGQYVLVA
VTDNGTGIQS DVLGKVFDPF FTTKVVGKGT GLGLSQVYGF VRQSGGHVKI DSEVDVGTTV
KIYLPRFAGE EAGSDLSQED IAAGASHQNE TILVVEDDER VRSMSSESLR ELGYTVIEAA
SAKEAIRTIE NGFVPDLLFT DVVMPDMTGA ELAAELSRRY PELKVLFTTG YTRNAIVHNG
VLDAGKHLLP KPFAIDDLAA KVRSLLDEI
//
