ID A0A2N5N9K2_9BACL Unreviewed; 1013 AA.
AC A0A2N5N9K2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B8V81_1260 {ECO:0000313|EMBL:PLT47036.1};
OS Paenibacillus pasadenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=217090 {ECO:0000313|EMBL:PLT47036.1, ECO:0000313|Proteomes:UP000234789};
RN [1] {ECO:0000313|EMBL:PLT47036.1, ECO:0000313|Proteomes:UP000234789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R16 {ECO:0000313|EMBL:PLT47036.1,
RC ECO:0000313|Proteomes:UP000234789};
RA Passera A., Marcolungo L., Casati P., Brasca M., Quaglino F.,
RA Delledonne M.;
RT "Functional genome analysis of Paenibacillus pasadenensis strain R16:
RT insights on endophytic life style and antifungal activity.";
RL Submitted (MAY-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:PLT47036.1}.
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DR EMBL; NFEZ01000003; PLT47036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5N9K2; -.
DR Proteomes; UP000234789; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
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; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lyase {ECO:0000313|EMBL:PLT47036.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 203..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 434..645
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 678..795
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
SQ SEQUENCE 1013 AA; 111516 MW; 5AB64168CB418A39 CRC64;
MGVVGIVVLF GIWLPLGIFS ERWGGQQPFR AEQGVIDLAG WDGSGRIALD GEWEFYWNEL
LQPGETPRGE RSWMEVPGVW SGSRAAGAER PVYGAATYRL RLTHLSEPGV YRIKKMNIRF
ASAIYVDGRL VLEDGKPALS AEAYVPGNSP GLAVVEIKGS EAEIIVHAAN YDYIDAGVPM
SLYFGKEEAI NAAHERSLIR ESAMAVVLAV IGLIHLVLFA AVWLYGQRDE PLLLFGLTCV
TMAVFNGLLG ERPLALLLDG LSFQTLYTIK DMSALAGFLV SLYLMMLLQG KGADRRLTKL
FALLLLGSLV LFPFLSIREY LPLYRVTILL EHVLMARVLW SAAARHLAAP RGQRYESLLL
LLAVLLLNLY SYGCLLFGMS MLGSLLISQI YLILFSLVVF LVIVYRFYEA FRDMERMHRK
LLRLDRQKDE FLSSTTYQLK APLQDIVHLA DSLAHADGPA PGSARSLALI AGTGRRLGYL
VQDLHDFSRL KHEDIVPEPR NLDLRSAVGS VLELHRFLLS GRPIELANGV PETLAAVYAD
EDRLEQILHR LVERAALRAE EGRIEVTAEE ELGFAVVTVD FDGRPRPAPD PDVAPCLAAA
DGEAADLALS ITRRLIELQG GLALQPLPGK EGRSFRFSLL LEKNPAASRK AAWPAAGEAA
AASETLVALA GGSRGQTVVL VAEPDAASRH AVCQLLAQEG LRAVSVRSAE QARAALALEG
ELSLVLLGVS LADGSGFDAL EQLRNRFSPS ELPVLMLTGR RREEERRLAL DLGANDYISK
PFEAEELLAR VRSLVKLRQS VREAREREIA FLRSQINPHF LYNALGAIAE LCVEEPEKAE
RLTLHLSGYL RGSFDFGQRD GMSTLGAELR LIEAYTEIEK ARFGSRLQVT LRCEADPALR
FPPLLLQPLV ENAIRHGLLS RPQGGEVKVT VVEREGYVHA AVEDDGAGFD AQAMLFRLEQ
PERIGGVGLW NVSERLRLLY GERLGMDSRT GFGSRLTFRI PASSRTSEPK EGG
//