ID F9RPP7_9VIBR Unreviewed; 1149 AA.
AC F9RPP7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VIS19158_19947 {ECO:0000313|EMBL:EGU35521.1};
OS Vibrio scophthalmi LMG 19158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870967 {ECO:0000313|EMBL:EGU35521.1, ECO:0000313|Proteomes:UP000004349};
RN [1] {ECO:0000313|EMBL:EGU35521.1, ECO:0000313|Proteomes:UP000004349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19158 {ECO:0000313|EMBL:EGU35521.1,
RC ECO:0000313|Proteomes:UP000004349};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU35521.1}.
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DR EMBL; AFWE01000144; EGU35521.1; -; Genomic_DNA.
DR RefSeq; WP_005596053.1; NZ_AFWE01000144.1.
DR AlphaFoldDB; F9RPP7; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR Proteomes; UP000004349; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000313|EMBL:EGU35521.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:EGU35521.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 632..848
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 920..1039
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 971
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1149 AA; 129720 MW; 2A4DEE4B0A2214EA CRC64;
MPEAKWAPYW GGIDKPSGLY HDFLITLTEV LNLELVYRGY DDFEPLFSAL DNHEVDVTIG
FASSELRRKH FQFSEPLISL KKIIWLADEK LQDQDPASWT WVCVRGGEDC EALEKFGVTK
FVTSNKLNVV AQMLRHNMAD ATITTLTEVN QYILDPRHSS GRIFLDYNMG SADIGLMMAK
DRTELKRTLD DAIENHQLAL TNIKLSNLYV LNEIAHWQLL QNQQKNSTIR YTIQEHSYPL
SYLDEQSGDI RGYVHDLTNL LERKTLFEFE YVPANGRNID EMLEQGLVDV LPGKNIFSVD
LETQLMTEQY TAVEYGLIKA KNSGTKRILA VLDRTNTLQP QIAEIERHEP VIVYSSAADM
LVDFNAGKIT HLLLDREIIE DYLYSNGTST SHQFESLPKP SYMDFDIPLV MSVRKDSALL
LNMLSRMLVI TDQSEIETLK QGHSKLFVNY GYSKDMVNYY VVLALVLVTV FVLIGIAVLG
VLSGRLKRTQ KINQLSQSEI SWLSTLLDNM PSIIFITDEN EEIVFTNSVY SDKVKDCQMN
AANSPVTPCG FTRDVLSTES NEVLYYDVSD GSLSGRYFHI RHQAIIHPEL GSNHRMTIVD
DITVEKQFEA DLQLSNQQAM QAIEARNHFL AVVSHELRTP IAAMLGLMEL LQFNLKKPQD
AELLKNAVHS AQRLKSQVNE ILDFSKIEAR QLQIDIRSHN VYQELCPSLR SFETVAKVKG
LNFVLDWHPS AIHQIEMDAM RVNQVLANLL SNALKFTKFG SITVCISNTE ELMTISIADT
GCGMTSAQLE TVFEPFVQAD KDISRRYGGT GLGMSITKNL IALMGGEINI YSDFGIGTTV
MCMIPIISKP STIHLGENLL ADTEREAQWL SAWLGKRVNA TNEHKCLGNI YPDRLFERWT
AMTRQDDIVA TKAIEDAQGL ILVADDDLIN QMLLHKQLAR LGVEFHIVSN GQEAQEYLEQ
FTEHVSLVLT DCHMPLMSGF ELAKSIKAQP DKFGSLPIIG CTAEDSRIIA EKAQACGMND
VLYKPYTLNE LSQILTQYIV AKPPTADSSE NMNWLNSGGE KEQMEMALVV FETFQKEIKA
LEKGSMDDKA IIHRIKGSSA LLEMNTLTEA AKQYEATDIV EDKADLKQSI IEELQAINSK
VKLWLETRQ
//
