ID W7YHN4_9BACT Unreviewed; 927 AA.
AC W7YHN4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JCM21142_1685 {ECO:0000313|EMBL:GAF02059.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF02059.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF02059.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF02059.1,
RC ECO:0000313|Proteomes:UP000019402};
RA Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA Iida T., Darby A., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT Anaerobe Isolated from Marine Mud.";
RL Genome Announc. 2:e00206-14(2014).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:GAF02059.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAMD01000005; GAF02059.1; -; Genomic_DNA.
DR RefSeq; WP_027473444.1; NZ_KI912107.1.
DR AlphaFoldDB; W7YHN4; -.
DR STRING; 869213.GCA_000517085_04161; -.
DR eggNOG; COG5002; Bacteria.
DR OrthoDB; 9796457at2; -.
DR Proteomes; UP000019402; 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; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:GAF02059.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW Transferase {ECO:0000313|EMBL:GAF02059.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..343
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 428..657
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 676..792
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 811..925
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 860
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 927 AA; 105441 MW; 70FF38F9A379A814 CRC64;
MKRTLIFVIG SIVFLVVSNI YYYNDTYNWQ IDTHKKVLEK DLSTCSEILS DYFSEVETSI
MLMLNEEELG GLFNIKLQNQ EVQKRIELLY NRYSSVLNKL EVYDNKGHFY ALSNDPNQNL
ITTYGKNSRI EEFKPRLVLN KKNIIYTQPL ASDSHIFGYA IFTINLHDFY DNLFRNFHIE
NHEFQWLINS NKEIIYSSFP DLQLVKPKLF PLQSKATPYI HMLKSNGRTF KVMSLAQNVP
LSKNNLTLVF SMPIKAITSS IARNSFFVAS ISFAVILLIA LAFYIHLSKN KEAILRSSQS
KGALNKILHY LPLGVILTDS ENKIKFVNKA ALQIFGHENE DVLIEQTASD QVLFERKKMI
RKDAVSQTSN RYIFNAGNEN EQVIVSEKNI FFNQESKNYI QFFIEISGIL PAAHPESSEK
AKTNFIANIS HELRTPLNAI IGMTDLLLST SKIEVAENEM LRVVKRSADT LLALINDILD
FSKIEAGKLE VESIPTDLAA EIQETVNAFT PIAQERNITL TTHLEEALPH DFMCDPLRFR
QILNNLIGNA IKFTPEGEVR LSVSRSTTLN GNPALTFCIS DTGIGIQKDK LVTIFTPFAQ
EDDSTTRKFG GTGLGTSISK NLVSLMGGEI WANSPSSISK NPHYPGTEFC FNLPFITKHI
NKGLDFSYIF SWAQITTLIV SDETLQVQNI IQNLLALGIN HKIMAPSQET ILFLKNKPSI
QLLVIDQRPD FNGLDFLQQI YNNNLHNNFL ILLQSSDFQT MNTQLGKRLG ADAYLRKPVR
LSNLRQLILR HFPNIKSQNS LTGKVVPDHI KILVAEDNPF NQRVAQNLFR KIGYEIDMVS
NGKEAVEKAK NNSYNIVFMD LMMPELDGFD ASKELKCRDE SCPIIAMTAN NDPQQRELAF
KAGMDDFIVK PAQKEEITRM LIKWCSY
//
