ID A0A0S8HJ24_9BACT Unreviewed; 673 AA.
AC A0A0S8HJ24;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMJ81_04045 {ECO:0000313|EMBL:KPK85175.1};
OS Phycisphaerae bacterium SM23_33.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703412 {ECO:0000313|EMBL:KPK85175.1, ECO:0000313|Proteomes:UP000054531};
RN [1] {ECO:0000313|EMBL:KPK85175.1, ECO:0000313|Proteomes:UP000054531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_33 {ECO:0000313|EMBL:KPK85175.1};
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:KPK85175.1}.
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DR EMBL; LJUF01000047; KPK85175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HJ24; -.
DR PATRIC; fig|1703412.3.peg.81; -.
DR Proteomes; UP000054531; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 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; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF17202; sCache_3_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..399
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 424..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 557..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 72552 MW; 3CD1C2F449EF44FD CRC64;
MTLRRRTVLS MLSVVAISGG VCTLIGGHLL WRYLGREAEN RVQQDLNAAR EFYDHRLEAM
AAALQYTALG ERFSEAVAAA ETGYLAPRLA AVRRSAALDL LYVADAQGRV IHRAHRPQAS
GDSVADDRLV REVLQGGGVT SGTMLVPVET LEKEDPSLAE RARIRILPTP KAVPSDSTEL
DAGMMLCAAG PVFGPGGRLV GVLRAGTLLS RNYELVDQVQ NTVFRGEQYA GKPLGTATVF
QDDVRISTNV LREDGSRAIG TRVSAEVHDH VLRQGKDWLG RAWVVNDWYV SAYAPITDVD
RKSIGMLYVG VLQRKFRDVA LNTLVTFALV TLAGLLAAGL VAWKLADSVS RPVRALVAAS
EAVARGDFSG TVPVSSSGEI SALMRTFNAM ANSLRERDEL LKQRTRLQLT RSERLAAVGR
LAAGVAHEIN NPLTGVLTFS HMLLRNAPEN SQQKEDIEAI IDATGRCRDI VRGLLNFSRQ
NEPQKSLSSL NEVLRRALNL TRNQARLNRI AVVEDMDADL PHLVIDPNQI QEVAVNVILN
AIDAMPDGGT LTVRTRAAAQ DSGAAEGERA AGPSGEARPA GPPGRWAEFE IADTGCGIPP
ENLEHIMDPF FTTKPPGKGT GLGLAISYGI VTEHGGQIRV ASELNRGTMV TVRLPVAPKE
KADEDEAAHT RGG
//
