ID A0A081KE38_9GAMM Unreviewed; 1132 AA.
AC A0A081KE38;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GV64_18295 {ECO:0000313|EMBL:KEI72414.1};
OS Endozoicomonas elysicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI72414.1, ECO:0000313|Proteomes:UP000027997};
RN [1] {ECO:0000313|EMBL:KEI72414.1, ECO:0000313|Proteomes:UP000027997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI72414.1,
RC ECO:0000313|Proteomes:UP000027997};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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:KEI72414.1}.
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DR EMBL; JOJP01000001; KEI72414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081KE38; -.
DR STRING; 305900.GV64_18295; -.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000027997; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027997};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 356..409
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 432..461
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 544..603
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 690..905
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 936..1052
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 985
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1132 AA; 125677 MW; 38D8ADFCDC7F3573 CRC64;
MSTSIRQKIT LFNLFPALVF YCFITFVFLY FSFRSASAEI GLRHLNQTLH YASLINGNIN
NVIHAGLALS LSVDSTSDIN ITSKISALFG DVFLIKSIAF ISFQNSGVLA VRDEESIYWK
RDDQQFIVSD VSQHYSVPES VFLSIIDRPD YSYDWYVNTE MVGEFDFYTS LLIKVSDDGS
DLVRFLRIDI DGSKLIDHPI KSDPRTRIII ADSGGSIVYA NGISLPKYRT VERFSRLGPC
QGYGEIFFPS EFSNPISEFF FRPVKNPPDP EMPCGFLKDI LNHVVNKKEA ASVRIFTRDT
YKWHTAVPIQ SVGWFFSYSI LESDLMKPVI RQAVLSASLI ALAMLLSIVC LWVVSGRITR
PLNELKDQMN TFGASPGDFA DSYSDSKDEA VSLGRSFVRL KNRLLNREEA LQNARAQNMG
NLVQQLRGSY FYFHLTSSGI ISYVSPSIVS VLGFSVEEFF GDIQKFLTES VINDSFKEIL
NHSPKGVWQE TFELEMSHKD GSIRCIEVSC AGHSNKGALT GNVPNQKVHS IECMGNDITH
RVRDTEKFKA LIAGSPDAIV ITDSSGVINL INSRVVDLFR YHECDLLGLP LALLIDPECR
SELALLKKLE PGSDSADSHC LDATLSRGFD RYGHGFPIEI SSNVLTTADG LIISIVFRDI
TQRKQIEGEL LKAKETAEKA SQAKSLFLSH ISHELRTPLN GVLGYAQLLL TDSDIPDKYR
ESLSSLEACG LHLLTMINDI LDITKIESGI VRSHLAPFNL QVTLDMVFAN VREVASAKGV
DLLLDINQAV QPELVGDNIK LRQVLINLIG NAVKFTDSGS VCVNVQLKDK QLQFEVLDSG
PGISSAEMAE LFQPFTQLKK GQECGGAGLG LSISYRLVKA MGGELQVESE VGKGSNFYFS
VPYLVSQVDS CKNGEAVPSS VKITTGIEGG LFSKRQILVV DDSFNNRDML VKALKSKSFH
VDAAEGGLEA VEKCRATRYD LILMDLRMPG FDGFDAARAI HGITKQRSIK IMAISASVSE
QTRMRIADAG FCGFIAKPVH FDELFICIHH HLEEADDQRL PSFLSDHCME EMINALKYSL
EIGDLESLEE QAERWTLEQG YGSIPTKIIE LCKSLDVQGL ESLYTSLLHS SP
//
