ID A0A0S8H673_9BACT Unreviewed; 609 AA.
AC A0A0S8H673;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMS25_09195 {ECO:0000313|EMBL:KPK80369.1};
OS Gemmatimonas sp. SM23_52.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK80369.1, ECO:0000313|Proteomes:UP000051975};
RN [1] {ECO:0000313|EMBL:KPK80369.1, ECO:0000313|Proteomes:UP000051975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK80369.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK80369.1}.
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DR EMBL; LJUM01000051; KPK80369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8H673; -.
DR PATRIC; fig|1703359.3.peg.3395; -.
DR Proteomes; UP000051975; 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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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 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.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW 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 63..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..360
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 373..594
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 66224 MW; D6284F6E02E4DAC6 CRC64;
MILWRSGAGS RNRGTSGLGG QTISEVNGNA VPLFDAGNDS AVKQELVSEA GERTYPRRVI
LRWVYLVRIG LAGGLFAGAA LAWSAASAVS PAQTLAASLA LVLTLIITPF SYWHTHVRRK
PAGSSFVYAQ AIFDVLLVTL VVHLTGGRDS VIPPFFILLI SAYTLVLPFR GGFLVTGLAC
MAYIAEVVWG QGTTVDTVVA LQLAIFVGVA LVVGLISHKL LETGAELTTL EHALEQLRLD
TGDILGNIPT AVLTVDGEGR LAYANPAAEQ LLRIEARSWM ERPVLDELAS RSTGLRRALE
RTRDFRIPVA SGEIEVKRDG ETIAVGISTA VLERREGRPS VTAMMRDISD RKRVEQLRQR
TERLEAVAEL SASLAHEIKN PLASISSSVQ QLELKEEADD DDRTLSRLIL KESDRLSRLL
SDFIEFARVR IERPQKLDLR EVTVHALSVV RQHPACSGDV ELETKFDPDP VLFEGDEDLM
HRVVTNLVLN AVQAGVSGRK TKVEVEVFNG GKEGLPEGFD IVNPIFLRVC DNGSGIPETD
LTRIFDPFFS TRTGGSGLGL AIVHRAVREH QGTVLVTSNE RTGTRFTICL PGNPPPASSA
VGEERRGEQ
//
