ID A0A2A2RZ81_9BACT Unreviewed; 1081 AA.
AC A0A2A2RZ81;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=B9S33_02180 {ECO:0000313|EMBL:PAW90072.1};
OS Pedosphaera sp. Tous-C6FEB.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=1982324 {ECO:0000313|EMBL:PAW90072.1, ECO:0000313|Proteomes:UP000218585};
RN [1] {ECO:0000313|EMBL:PAW90072.1, ECO:0000313|Proteomes:UP000218585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tous-C6FEB {ECO:0000313|EMBL:PAW90072.1};
RA Cabello-Yeves P.J., Ghai R., Mehrshad M., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Genome diversity of Verrucomicrobia from freshwater lakes.";
RL Submitted (APR-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};
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:PAW90072.1}.
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DR EMBL; NEUT01000009; PAW90072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2RZ81; -.
DR Proteomes; UP000218585; Unassembled WGS sequence.
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; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 562..644
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 635..686
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 847..1062
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1061..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 545..572
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1081 AA; 120409 MW; 0A23AF9F0AECEB0A CRC64;
MQEREQAASF EWCGWQVAPF FRSGSDDISG GGKTCFARWL MSVTLPAMQL VPHSSRPALT
AALACVALGA FSLAGWWLKV PPFDRWVASE MFMKANSALG FIFAGGALAL NVTPSIRRWE
WLVAGMLAGL VTLLGGLTTV EYLLGRDLGL DELLVNDVVG DELARPGRMS INGAIGFLLT
GSALFLVNGQ PQKRHRPMMV GLLACVLFGL ALFSLSGNLL EMPTSYRWEG TKPMALTSAL
SFMTLSAGFM ILAHGWSQRD GLALVRWMGP AVGTGVLTVT LLLWQALRAQ EEREIDRVMA
QQVREARQLL VTQAQARLLT LTRVARRWES QLVRRPGNWD FDAQLYLSHY PDLKALVWLA
DDLAVREAAP RSIRGKLLQL QNEPNSKPAA WVQAVRQRPE GSVTPTVDLG GERGFLMVVP
MTQGTNSAGF VVGAFQARAF VETALGPVRR GHWFKLTEQG QEIFRSSSSP AEVARPHVAD
LRLGDAVWEM RAWPTSTTLA ELHTPLAVIA LSGGSTLAIL LGLAIQLTQT ARARESEVRK
INRTLQAEVS ERKQAQDLLR ESQQRLQAIL DNSFAVIYLK DAQGRYLLIN QRFETLFHIQ
REAILGRTDH DIFPELMAEA FRANDQQALK SRTALTIEEI APQDDGLHTY VSIKFPLLDA
RGEPYGVCGI STDITERKRA EAELRASHVA LEFAHHRLRG IIEGTQDQIA ALDLRFRFIT
FNTAYKEEVR REFSREIEIG MRLSDPLAHV PEEREEQLAL WARALRGEAF TVERSRRAGT
EAEQHFEISF SPIRNETGEL LGAAQHVRDI TARQKAGAER ARLLEELARR NGLLEAANRE
LEAFSYSVSH DLRAPLRHMD GFAGLLQRTA EAKLDEKERR YLGLIMEAAK RMGRLIDDLL
EFSRMGRAEL RHEDVDMNRL VQTVLRDLEP DTAGRNINWQ IGPLPVVRGD AGLLRQVWMN
LLANAVKYTR PRAEANIAVG CDSRQPLEHA FFVRDNGVGF EMKYATHLFG VFQRLHRAED
FEGTGIGLAN VRRIVARHGG RTWAEGTPNV GAVVWFSLPQ STQQTQPPGA QDGAGEIVAT
K
//
