ID A4BZQ6_9FLAO Unreviewed; 862 AA.
AC A4BZQ6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PI23P_08485 {ECO:0000313|EMBL:EAR12649.1};
OS Polaribacter irgensii 23-P.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR12649.1, ECO:0000313|Proteomes:UP000003053};
RN [1] {ECO:0000313|EMBL:EAR12649.1, ECO:0000313|Proteomes:UP000003053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23-P {ECO:0000313|EMBL:EAR12649.1,
RC ECO:0000313|Proteomes:UP000003053};
RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR12649.1}.
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DR EMBL; AAOG01000002; EAR12649.1; -; Genomic_DNA.
DR RefSeq; WP_004570317.1; NZ_CH724148.1.
DR AlphaFoldDB; A4BZQ6; -.
DR STRING; 313594.PI23P_08485; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_398939_0_0_10; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000003053; Unassembled WGS sequence.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE 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 PRINTS; PR00344; BCTRLSENSOR.
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; 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}; Kinase {ECO:0000313|EMBL:EAR12649.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003053};
KW Transferase {ECO:0000313|EMBL:EAR12649.1}.
FT DOMAIN 225..264
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 277..332
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 486..556
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 559..611
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 640..858
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 141..218
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 423..457
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 862 AA; 97840 MW; 4A84C081487A8DD3 CRC64;
MSKNSKETLI TKRTALKKTL IQPSDENHYE ALYDSMSEMV EVIELIYDEK QQPVDFYIRN
VNISFAKLLN KTKEELIDKK ITAVVGIIED YWLSSFASVD KTGKPLSFKS YGAEFDKYYF
VSAWKIREGR VGISLTCITA NEKAEIKLKK KIEKEKNARN KSEKQLKKKS LELQNSLDAL
HSLNIKLAFQ NQEKDERAAE LANIKIELEE QIICLNEAAI VSETDAEGNL IFVNDNFCKM
FGYQRKELIG KSHAVVKSGK HPSNFLKNIW STINIGKVWK GEIINKAKGS TDFIWLDMTI
TPFTDIHGKI VKYVGIQFDI TAQVKQRQAL LKQAEKLASV NLKLASQNKE KDKRVKELAK
AMYDLSYQNE EKDKRSKELI LAKEEKEKRA RELAIANIEL AFQNKEKEQR ANELAIANAE
LAFQNKEKDK RAHELIIAKE EKEKRAKELT IANAELAFQN KEKDKRGNEL IIANKEKDKR
VEELAIAKEL RQFIETSSTP IFGIDKTGLI NEWNQASERV TGYQKEEVLG INWLIFTPKK
SEKGARQVLY MVLKGKQTAN FEFAIVAKDN KEVILLVNSS TRRDIHGNVT GVLAVGQDIT
ELVGYRNELE IKVKERTLKL NQALEKQKEL NELKSKFVST ASHEFRTPLT AINFAAGSIK
KYWGKMEPGI VEQKLYKIEN QVLHMTRLLD DVLIVGQAGA GKLKNHPSNV HLGDFMKEII
EEVSISQEQS HQIALIDPNN LKENIIFIDK KLGRNVFTNL ISNAVKYSGN SKKITVEFSS
EKNNIIISVT DFGIGISKRE LKTIFHPFSR GQNVDLIQGT GLGLSIAKEA IEIMNGEIII
KSAIGKGTTF TAKLPKLNNN DV
//
