ID A0A1S9PKT4_9SPHI Unreviewed; 596 AA.
AC A0A1S9PKT4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BC343_00310 {ECO:0000313|EMBL:OOQ61557.1};
OS Mucilaginibacter pedocola.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1792845 {ECO:0000313|EMBL:OOQ61557.1, ECO:0000313|Proteomes:UP000189739};
RN [1] {ECO:0000313|EMBL:OOQ61557.1, ECO:0000313|Proteomes:UP000189739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBZ30 {ECO:0000313|EMBL:OOQ61557.1,
RC ECO:0000313|Proteomes:UP000189739};
RA Huang J., Tang J.;
RT "Genomic analysis of zinc-resistant bacterium Mucilaginibacter pedocola
RT TBZ30.";
RL Submitted (JUL-2016) 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:OOQ61557.1}.
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DR EMBL; MBTF01000001; OOQ61557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9PKT4; -.
DR STRING; 1792845.BC343_00310; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000189739; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000189739};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..446
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 468..586
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 517
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 596 AA; 66194 MW; B0B535AEECF05CC8 CRC64;
METPISVFNF SLKKVLGMEP DNLKKARIKI VYTILLLSIL KIVVLLPMVH QTIQQGQLYR
VIAALVLYVG LAKYLLYKPA HIGIISHGMI ITGVIAIWAN LLHFQQGVNL VTLQFVFMVT
FVSYYLIDSR YAIIYSIFSI APLMYILATS GRDKWEVGFV PQELPSPGFE TIVFMNFCTM
VLVHYLFYCA FRANVTEKEE LNKQLEAQVA ETKALAESRS VFLSTMSHEL RTPLNAVIGM
ANLVKDTATE EQTENLDILE FSAMSLLTLV NDILDYNKSE NDKIELEAIP VSLPDMLHKV
CSGLKLKASE KGLDIILDVD DRLKSNWVMT DPTRLTQIVY NLVGNAIKFT ERGRVNIRAT
AMAATEEYIP VQFTIADTGI GIPLNRQEAI FDPFTQASAE TTRHYGGTGL GLAIVKRLLK
LFGSDIGLQS KPGYGSTFTF NIKFELYHGA INPITVKPAT ASTLEGLSVL IAEDNPINSL
LLVKLLTKWN AMCVVAVNGR DAVEKLKQSS FDVVLMDVHM PVMDGYQATK LIRELPDPVK
ARVPIFALTA SVAHNISGKV ALSGMNDYLT KPFQPALLFQ KLAPLNKFRE GSVMVG
//