ID A0A0S7XH99_9BACT Unreviewed; 921 AA.
AC A0A0S7XH99;
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=AMJ46_00955 {ECO:0000313|EMBL:KPJ61675.1};
OS Latescibacteria bacterium DG_63.
OC Bacteria; Candidatus Latescibacteria.
OX NCBI_TaxID=1703781 {ECO:0000313|EMBL:KPJ61675.1, ECO:0000313|Proteomes:UP000051457};
RN [1] {ECO:0000313|EMBL:KPJ61675.1, ECO:0000313|Proteomes:UP000051457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_63 {ECO:0000313|EMBL:KPJ61675.1};
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:KPJ61675.1}.
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DR EMBL; LJNC01000002; KPJ61675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XH99; -.
DR Proteomes; UP000051457; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
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; 5.
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; 5.
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; PF08448; PAS_4; 4.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 74..146
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 149..200
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 201..271
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 391..446
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 447..518
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 521..573
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 644..695
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 715..921
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 679..706
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 921 AA; 104101 MW; A3D58934E09A16FD CRC64;
MLLGVGVAVA YWLVDSVVHS FLFHECSFSE AFLSLTPREI WMRLLPVLIL LVSAFILQSL
FNKQDKAERT LRENEEKFRR IFESAGELIG YVGEDGRILD VNPKIEEMLG YKREELVGKK
ISELDIYPEG VLSIVMESFG RVVKGGPSTG RRVELRHKDG RSIFVESSTV ALQSEGEIEG
ILFIMRDVTE RARIEDVLRE SEKRYRHLME SITDAVTVVD REWRQVLVNS AAERFLEMPK
EKLLGTRVTD ALPGVEKTEF FKTMQRVMET REPAVVSGQY SFESGRVGWY EVRVYPAEEG
ILCITTDITE RVQAEEKLRV GEDRWDCLTS NTDDTIIIAD RNRVIEYINK PLAPHTFEDV
IGKKLSDFVS KEHHDLLEES LRRVFEEGEP VEYEVSLDTK KFSPGIGTLW FSTSVVPMTS
SGVVSHAILI ATDITERKKA DEALRESEKR LLGIINSSPD PILVCDVAGT VVQCNEALLK
AHGLRSETDL LGQSVLTLIA SGSRQRIVEV LGELPEQGVV RDLELTLLRK DGTEFPAEIS
AGLVRDQTGR AKYLVGVAKD VTKRRKVERE LWDATEKWTS LMENTSDIIT VMDRDGRVQY
TNRALAPLAP EETIGRTMFE YIGKEQHGLL AQKLQRVFET GETQSYEMRS DITGVGPRWF
SSKMIPVKHD REVVSVITIA SDITERKRVE EERERLRQQL AYAEKMESLG HLARGVAHEI
NNPLTSVLAT AELILDEMCD ENVSRSDIEQ IVREARRIQD TIRSFLGFAK ARDFVFEERD
INAIMETALM AVGKAQLRDC EVVTDYDDSL GKVKVSRFHI QEVFVNIIAN SLHSMRDGGK
LTITTGQSND SVVVTIKDTG AGIRAEDLDR IFEPYFTTRE KRGTGLGLSI CRDIVMRHGG
KIEVRSEGPG RGAEFKVFLP R
//
