ID A0A372IK12_9BACT Unreviewed; 785 AA.
AC A0A372IK12;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=D0Y96_16435 {ECO:0000313|EMBL:RFU15276.1};
OS Paracidobacterium acidisoli.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Paracidobacterium.
OX NCBI_TaxID=2303751 {ECO:0000313|EMBL:RFU15276.1, ECO:0000313|Proteomes:UP000264702};
RN [1] {ECO:0000313|EMBL:RFU15276.1, ECO:0000313|Proteomes:UP000264702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G-K13 {ECO:0000313|EMBL:RFU15276.1,
RC ECO:0000313|Proteomes:UP000264702};
RA Gao Z.-H., Qiu L.-H.;
RT "Acidipila sp. 4G-K13, an acidobacterium isolated from forest soil.";
RL Submitted (AUG-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};
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:RFU15276.1}.
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DR EMBL; QVQT01000006; RFU15276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372IK12; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000264702; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 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; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; 2.
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; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
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; 2.
DR SMART; SM00091; PAS; 2.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 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}; Reference proteome {ECO:0000313|Proteomes:UP000264702}.
FT DOMAIN 8..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 228..280
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 367..419
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 416..482
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 549..764
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 766..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..158
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 785 AA; 87171 MW; 17782BF9388E6E64 CRC64;
MTVNEKVNIL MVDDQPGKLL TYEAILAELG ENLIKAASAR EALEVLLRTD IAVVLMDVSM
PDLDGFELAG LIRQHPRFQK TAIIFISGVH LSTEDTINGY RRGAVDYISV PVIPEVLRAR
IGVFVELHRK TRMLERLNND LERRVEERTE ELRQSEDQFR TLANSIPQLA WMAQADGTAF
WYSQRWCDFS GVSMPVLLAT GWAFLCHPDH ADRVAGGLGS AVVAAQPWED TFPLRSRDGE
YRWFLCRAVP IVDSQGKVAR WFGTATDVTA QIAAEEHIHL LNRQLELRVA ELETIMRVLP
VGVAISADAS SANATMNPAF RAIFGTNGIR HLNGSGPADG VEKSLTEHAH LPFLFMNDVI
HAGRPVMDAE MQLQGSDGLE KYVLASASPV IEPSGNVRGA VGVFFDVSHR KRLENTLRER
AELLELASEG IMVRDMQGVI RYWNSGAESC YGWRREDVHG QDVHALLQTV FPVSRDELNS
ILLREGSWRG KLSQRTSSGH EVVVDSHMVL DRETGSILEI NRDITRELRA EEALRQAEKL
AAMGRMAGII AHEINNPLEA ITNAFYLLRN HPSLDDQAKY YADMAEQELQ RASHITRQTL
SFYRESKQPV PVSLPEVIES VLELQQRGLQ SSGIDLQKQY RSGGVIYAHP VELRQVFLNL
IGNAVQAMPG GGTLRIRISE ATDGLTGRRG IFLSVIDTGV GIDPENAEKL FQPFFSTKST
KGTGLGLWIS KGIVQKYEGR IAFRSQYYKG RQATCFRVFL PAETTHSSAK SGGKPAADSV
AVKVS
//
