ID L8JUW1_9BACT Unreviewed; 694 AA.
AC L8JUW1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C900_01150 {ECO:0000313|EMBL:ELR72771.1};
OS Fulvivirga imtechensis AK7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR72771.1, ECO:0000313|Proteomes:UP000011135};
RN [1] {ECO:0000313|EMBL:ELR72771.1, ECO:0000313|Proteomes:UP000011135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK7 {ECO:0000313|EMBL:ELR72771.1,
RC ECO:0000313|Proteomes:UP000011135};
RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT "Genome assembly of Fulvivirga imtechensis AK7.";
RL Submitted (DEC-2012) 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:ELR72771.1}.
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DR EMBL; AMZN01000015; ELR72771.1; -; Genomic_DNA.
DR RefSeq; WP_009578824.1; NZ_AMZN01000015.1.
DR AlphaFoldDB; L8JUW1; -.
DR STRING; 1237149.C900_01150; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 973200at2; -.
DR Proteomes; UP000011135; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13424; TPR_12; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00028; TPR; 6.
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; SSF48452; TPR-like; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011135};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..694
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003993456"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 487..694
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 432..480
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 694 AA; 79218 MW; 86B0388764A46B36 CRC64;
MNAYKVIRLA LFFILLSEFV QAQSDSFPAA FEELKHGSQK NIRAYFDSLR NISSNDKESI
HLSLLSYGHT HDRPFIEALA LRNLGHIYWE KNEPVRSVTN LRQASEIAND LKDIELESEI
LMDLAEIFNV HGGEEKAMEY YLKAYPLLLQ TDKMRAARAQ NAMATLSYGV GNIKACIKYC
QAGMTLFESQ PIDALNKVDQ KVYMQLLNTL GIAYRETNNY DSAIHYLNAS KDLASAIDDE
FWKTLTLGNM GIIYTRTGDY AKALPLMEQD MVISKKFNEW LSASSAAVVI GNIHREMGSL
DAAKIYYDSA MIIAKANNLV PRIAPIYHNN LAKWYALKND FQHAFYHQEK YTYLKDSAQN
KNQQVELSRI KATYDFDSKL SQIDLLTRNN ELQRQKIEYR NIIITASISS SLVIFIIALL
LYKNLNARKK DNELLSAQKA RIESQSKQLA DQNRIIQANN DNLEIEVSKR TRKMEQLNRE
LDTFLYRASH DIRQPIATIL GLENLARWYA KDNHLSEILL RVNSTAMSMD NMLRKLQMSY
EVNRQPEKLI SLEVRDLIFQ VVAANQGEIN LRKINLQFDV KAQYINSNRE LLKIIVQNIL
ENAILYSNEA TPEIHITGAP ASDEYIIKIT DNGDGIPKEY IPSIFNAFFK SNIKSKGNGL
GLYLALKAAN ILETKIEVHS EPAKGSQFVL HIPI
//
