ID A0A1Q8QMW2_9FIRM Unreviewed; 594 AA.
AC A0A1Q8QMW2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DSOL_3911 {ECO:0000313|EMBL:OLN28676.1};
OS Desulfosporosinus metallidurans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1888891 {ECO:0000313|EMBL:OLN28676.1, ECO:0000313|Proteomes:UP000186102};
RN [1] {ECO:0000313|EMBL:OLN28676.1, ECO:0000313|Proteomes:UP000186102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL {ECO:0000313|EMBL:OLN28676.1,
RC ECO:0000313|Proteomes:UP000186102};
RA Mardanov A., Beletsky A., Panova A., Karnachuk O., Ravin N.;
RT "Complete genome of Desulfosporosinus sp. OL.";
RL Submitted (SEP-2016) 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:OLN28676.1}.
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DR EMBL; MLBF01000040; OLN28676.1; -; Genomic_DNA.
DR RefSeq; WP_075366332.1; NZ_MLBF01000040.1.
DR AlphaFoldDB; A0A1Q8QMW2; -.
DR STRING; 1888891.DSOL_3911; -.
DR OrthoDB; 505470at2; -.
DR Proteomes; UP000186102; 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; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF34; SPORULATION KINASE A; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OLN28676.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186102};
KW Transferase {ECO:0000313|EMBL:OLN28676.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 388..592
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 594 AA; 67804 MW; 045C9B00B4CAB9CC CRC64;
MILNIKNIIK KQSIIQLTLF KIIFSIFTFL IIFIFSYGQS FLKNQALQFN YNLLLSALSV
QSKIQPQISL IGELKRDTNL KKNQKILKID SIVQSIINNV NDNLVGYYDV ELDLIVKNQN
NIEFSFDEIR SIMGSISENN LSTNNKLLGV NIPIYDKEKL VGYVWAYAKK TDYVLVSFYE
LSEIVILVLT LLALIIFLIR KYIKQIESCL DEFCIMIINN DCEQDQILTK LPELVPVLNK
ITTYTDDLKK INQKLESSTL KTNKIMEGIS DGFYALDRDW KFTFVNNKLK IVISEENTEL
IGKSIWEVFP QVIDTLSYDK MQEAMSQNQS VHWEAGGFAR PDQNHEYHAY PYKEGLTVFV
RDISELKRQQ QEFDRLERLN LIGQLAAGIS HEIRNPLTTV KGFLQIFGTK TKYSEDKEVL
ELMITEIDRA NAIITDFLSL SKVSLDNIKL KNINETILKL FPMLQADAFN SNKQVVLDLN
VLPDIMINEN EIKQLILNLV RNGLEVTPEK GRVLINTYPM GDKVVLAIKD QGTGIPQEIQ
EKIGTPFFTT KETGTGLGLA ISIGIAQRHE AVFNFETGKN GTIFTTIFPT LTAN
//