ID A0A0P6X0L6_9SPHN Unreviewed; 1042 AA.
AC A0A0P6X0L6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SZ64_10075 {ECO:0000313|EMBL:KPL68431.1};
OS Erythrobacter sp. SG61-1L.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68431.1, ECO:0000313|Proteomes:UP000049978};
RN [1] {ECO:0000313|EMBL:KPL68431.1, ECO:0000313|Proteomes:UP000049978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68431.1,
RC ECO:0000313|Proteomes:UP000049978};
RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA Pandey G.;
RT "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
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:KPL68431.1}.
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DR EMBL; JXQC01000003; KPL68431.1; -; Genomic_DNA.
DR RefSeq; WP_054530701.1; NZ_JXQC01000003.1.
DR AlphaFoldDB; A0A0P6X0L6; -.
DR STRING; 1603897.SZ64_10075; -.
DR PATRIC; fig|1603897.4.peg.1937; -.
DR Proteomes; UP000049978; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR001610; PAC.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 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 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; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 437..478
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 510..563
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 563..631
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 638..691
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 709..929
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1042 AA; 115394 MW; 7B4551EC757AF9FA CRC64;
MRLSQKAILL IVPLALLAFG LLTWMAYDAA RDREVIRSVD LLRTARVEAE TEVERRITEI
RKTEARAREL MRLALEDEIG SPARFDRLFP KKGDGSRRGA EFLWTGKAQQ GIPARGIGAF
VSGENVPEDR RKTILAAYDT LRSMTEGLGP TIESLYFYTT TNDLVMYAPR REDQLKFYRT
SAPANLNFQD REFATITSPK VNPSGRMRCT SLTQILYDQG GYMWTTGCMT AMRTGGRHLG
AWGSSIPLDS LLKDLQTDVP GVQNIIIADD GKLIRHPDYT VQSSRETERF LDLDSTKEPR
LQALWHFVQK ERRNDFEAYS PELDAYVSMA RLGQPNWVVI SLIPGERVRS AAFGLALPLL
LAGTIGALVF IAVALWFINR QIARPVAAMA VRADAIAALA NRKEGEVPPE PPVDEIERLG
LAFHEMEQRI DWERANLSRS FDTLVDAVSD YGIVLLDKDG RIIRANQGAH RLLGWNPDAR
PEGLAGVFGP GGKGEWRYME FLVRAARDGR ISEDAVRYRS DGSEFWANDS ADALIGIDGE
ALGFAYIIRD VTGERERMMQ IEESVSFLEL AESTAQLGHF LVDTQRLTVR LSKWVCDLYG
YPHGTEIGFR DVGKLIAPED RRRVLEVLQR ARMQLEPFET TFDLIDKQGR RRTAFVKASP
LSAGMGGVPR GLFGIARDIT ERTVAEARLV AARDAAQAAA DMRRDLLATV SHEIRTPMTG
ILGLLDQMKR EQSASKRALA LKLIEDSADA LMRVLDDVLQ DAKIESGSFV VEKIEFDTQD
LMLRVTELFR PLARRKGIGL TMSDDCGRRL VGDPARIQQI VANFLSNSIK FTSNGGVSLH
CSCRPLNVPD MLELIVEVED TGIGIPQDRL SQIFQSFEQA EASTERRFGG TGLGLAISRR
LAQAMGGTVE VESTEGKGSR FTLRLPQGMA QGADLRRPGK GKDALVVSSS ASARVMAEAL
VAELGYSTKG SGNLCNSAGD EALVVFDADE TDPQDWEGIA PGQLLALVSQ EKTALRQRLA
EAGIRMIFKP IELDALRQAV QQ
//
