ID M7N0T4_9BACT Unreviewed; 711 AA.
AC M7N0T4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cph1_11 {ECO:0000313|EMBL:EMR02273.1};
GN ORFNames=ADICEAN_02582 {ECO:0000313|EMBL:EMR02273.1};
OS Cesiribacter andamanensis AMV16.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC Cesiribacter.
OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR02273.1, ECO:0000313|Proteomes:UP000011910};
RN [1] {ECO:0000313|EMBL:EMR02273.1, ECO:0000313|Proteomes:UP000011910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR02273.1,
RC ECO:0000313|Proteomes:UP000011910};
RX PubMed=23682146;
RA Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL Genome Announc. 1:E00240-13(2013).
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:EMR02273.1}.
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DR EMBL; AODQ01000065; EMR02273.1; -; Genomic_DNA.
DR AlphaFoldDB; M7N0T4; -.
DR STRING; 1279009.ADICEAN_02582; -.
DR PATRIC; fig|1279009.4.peg.2618; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9766459at2; -.
DR Proteomes; UP000011910; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011910};
KW Transferase {ECO:0000313|EMBL:EMR02273.1}.
FT DOMAIN 218..271
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 297..348
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 349..419
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 422..475
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 493..710
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 194..225
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 711 AA; 81057 MW; 804761A14165A1D6 CRC64;
MERLTRLHEP APDGFATTRS LALPIRMEKL DQETLLIDPR IQQLSQLTVD IHQQSTLQEK
LAIITRQVRE IIGCHQSVTR MTANEAGGQE ITEVSLSDKY ARWREYAAPI DGSGIYSLIC
RFNKPMRLSQ QELEQHPAWK GFGQHRGEHP PLRGWLAAPI LGQGGSIGLI QLSDKYEGEF
TAEDELILVQ LAQIASISIE NARLLERLQT ALQEKEKAIK LTRTITDNAT SALVMMDATG
HCTYMNPAAE KMFGYSFEEI RQKPLHYQIH HHRPDGSHYP LEECPIDRAL PENFDIRAHE
DVFIRKDGTY FPVLCAASPI FEGGVPVSTV IEVRDVTEER RRQEEILEKI EWIRFLLDAM
PQKVWTASAN GSVDYMNKNW LSYTGIASEA LLDWGWQQII HPEDWELTRQ KWQAAIDTGE
NFQIEHRFLR HDGEYRWHLS RGLAYKDSTT DTIILWVGTN TDIHDHKIAL ETVAKSNVEL
TRTNNDLDNF VYTASHDLKA PVMNIEGLLH ALERVMKPKA GADKEVGMIL DMIQQSIGRF
KNTIGHLTEI SKIQKNLEED VTEVEFASLI REVLLSISKQ VRDTRALIKV DTSGCEQLRF
SQKDLHSIVF NLISNALKYH SPERKLEIEI TTRQEGAYAV LSVKDNGLGF RQEQAEKVFS
MFKRLHNHVE GSGVGLYIVK RIVDNAGGTI KVESEVDRGT HFQLYFKLAT P
//
