ID F9RUX7_9VIBR Unreviewed; 833 AA.
AC F9RUX7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VIS19158_15574 {ECO:0000313|EMBL:EGU30144.1};
OS Vibrio scophthalmi LMG 19158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870967 {ECO:0000313|EMBL:EGU30144.1, ECO:0000313|Proteomes:UP000004349};
RN [1] {ECO:0000313|EMBL:EGU30144.1, ECO:0000313|Proteomes:UP000004349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19158 {ECO:0000313|EMBL:EGU30144.1,
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
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:EGU30144.1}.
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DR EMBL; AFWE01000220; EGU30144.1; -; Genomic_DNA.
DR RefSeq; WP_005599654.1; NZ_AFWE01000220.1.
DR AlphaFoldDB; F9RUX7; -.
DR eggNOG; COG0784; 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:UniProt.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:EGU30144.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EGU30144.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 464..679
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 713..826
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 762
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 833 AA; 93770 MW; 033DF591F7A390D9 CRC64;
MFEPFVHPIL LLLLGVASLV LGWTVYFVYS LRISGGTFER KISIPYLFYS LSVFAWILSN
AFFYSPLLLQ ADNDAVVFMA LFANLASSSA FAFAYLVTRQ LVTDIDSTLS RYLQNALFIV
LISAAIYWNH RAGSTVEGVS VYAIGRFNIQ LGEQAATFFL SAMALIVLSF RNILLYSRHA
RPLQHIKSLY MLFGISVFMV STIVIHAFIP LIWKNFTLSW LPPALAVTEM LLMGYALVTS
RFYSNRHILF SLLSVLLACI TVALPLVLLI NSISLYDAAI IVPLSCLVTG LAWRVIFRTT
THLASQLVYG QALSPTQKLN ALTREFQKST HSAISQIAQT LDIDQHDLQL VYNLQDEKAY
TSQLYNQNSV IIFEEIEEQV LTHSSVSSLL KQLHVKMKRE GVALVLPIFD HEDQMSHLLI
ARQKCSGHLY FCEEIHALQY VLKKAQGYIN ADKKVHQAQA LANSIAHEMR NPLAQVQLQF
EQLDTKLQIS APKIELEQEL IKGKVAIERG RQLIDIILRE VNDASLEQEP AVQTSIKQAI
EQAVERYAFE SDEMRQRLHI SIEQDFHAKI NDTLFNFVIF NLLRNASYYF DSYPQSHIDI
RTIVGKYEHF LVVRDTGPGI PKSLQARIFD DFYSHNKSGG SGLGLGYCRR VMKAFGGSIQ
CYSKLGKFTE FHLSFPVDSL VSPANSPVIT EENTAFVPIN IGKQNDNADN EYTILVVDDK
EVQRQLVKLL LNQLGYDAIL ANNGQVALEI IQSNRVDLVF MDIQMPVMNG FEAASIIKQT
FPQIPVYALS GESGQRELDK IRQIMDGHLT KPTSKEALLA TIQGEKQKTP IGA
//
