ID U3CF00_9VIBR Unreviewed; 1128 AA.
AC U3CF00;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VAZ01S_054_00330 {ECO:0000313|EMBL:GAD76868.1};
OS Vibrio azureus NBRC 104587.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219077 {ECO:0000313|EMBL:GAD76868.1, ECO:0000313|Proteomes:UP000016567};
RN [1] {ECO:0000313|EMBL:GAD76868.1, ECO:0000313|Proteomes:UP000016567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104587 {ECO:0000313|EMBL:GAD76868.1,
RC ECO:0000313|Proteomes:UP000016567};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio azureus NBRC 104587.";
RL Submitted (SEP-2013) 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 -!- 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:GAD76868.1}.
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DR EMBL; BATL01000054; GAD76868.1; -; Genomic_DNA.
DR RefSeq; WP_021710614.1; NZ_BATL01000054.1.
DR AlphaFoldDB; U3CF00; -.
DR STRING; 1219077.VAZ01S_054_00330; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2770; Bacteria.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000016567; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17538; REC_D1_PleD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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 PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000016567};
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 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 377..430
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 466..684
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 723..839
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 418..456
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 772
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1128 AA; 127604 MW; 5FC11B3E746D9F51 CRC64;
MFKFYKNQKF KRLQSTLMSA FLVLSITPLT IIAIFFLHSH SQDLQEQSTS HLLSVRDTKQ
QQIIDYLTTK ETEVMGFVRS ELAYASGGRF YGLVNAFSQL GQNMDEAREN AQQRYITSSG
DQIKTSTLPE SNNYLGSERY RLLHKRYHWA YLELLKRSDF TDILLVDLDG NVTYSANKDD
NYGTNLLTGH YKDSILGQTF KRLTEDVSKN RKSNEDYTPV VFSDFTPENG ESVAWMGAPI
IQQGYLHSYA MFRLPNNGIT KLLADNKHNV SIEALLVGNN NNPITSNIKP KEIENSAKVI
AQSLSGNIDV MTYGNGQQEE IIAAFTPIKT HGVTWALIIQ LPEKEAFARV HQLQKLFVIA
MVVAILLVVI ASHYLSNFIT APLLQLTWGA EKVSAGDLDD TIFDTHRKDE IGRLAQSFQR
MQRSIREKIQ TIKQQNEELE SNLTLIKKQN EDLQLANKLK DEFLATTSHE LRTPLHGMIG
IAETLVSGAN GVLPKHQQYQ LDIIIKSGQR LANLVDDLLD YHKMRYGNME IQKSAVSLAS
ATRLVLELSN HLLGNKTIRI INQVPADLPP VSADPQRLEQ VLYNLIGNAI KYTPEGKVVI
SATVVDEQIR VQVVDTGQGI PAEALEHIFE PLIQASHDTG RYRQGAGLGL SISRQLIELM
DGSLYVSSQP MVGTTFSFTL PRASEDEIQA TRHLDQYDHF QAPEVYLETA QPLTLPESSD
GPLLYIADDE PVNLRVLESF LRIEGYRIRT ACDGPDIIEL VEKEKPDLLL LDVMMPGMSG
YEVCSQLRNM YDHAELPIIM LTALSQTEER LKGFEAGAND YLSKPFSKHE LAARIQAHLT
ASKAEMRHVE NQLLESELRK RAEVEASLLE TQGRLLEQLE SAPEAIICLR EDHRIRFANE
AACKLFKRNL EQLKRSSADE LIAPKYLTVT QSHYCGNIDI YIEDIRQSIE ADILKLPEES
GLDVMYIFNI GGGINATRIH NLETAVEVLS CYAFDGDKEQ LQKLKELGGE FTRLADKALG
SKKDKQELLR EILVDTITHA LAYWESSTGE SKFAFAEQSG LWRVYLDRST LQTRTLDKYM
RLETLPKTPR WRTVLSSIEF ILEHCKEQSP ERSYIEAQKN KLQRLLTN
//
