ID D5BCD3_ZUNPS Unreviewed; 815 AA.
AC D5BCD3;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=ZPR_4458 {ECO:0000313|EMBL:ADF54759.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF54759.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF54759.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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};
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DR EMBL; CP001650; ADF54759.1; -; Genomic_DNA.
DR RefSeq; WP_013073819.1; NC_014041.1.
DR AlphaFoldDB; D5BCD3; -.
DR STRING; 655815.ZPR_4458; -.
DR KEGG; zpr:ZPR_4458; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_50_10; -.
DR OrthoDB; 1046984at2; -.
DR Proteomes; UP000001654; Chromosome.
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 Gene3D; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADF54759.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ADF54759.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..544
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 572..687
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 724..815
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 542..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..136
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 235..267
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 781..812
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 621
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 763
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 815 AA; 93446 MW; CC21712516892E87 CRC64;
MQNTKRSITL KVVAGYLLIA VLVVVAVWFI YNRVVIFSHM AQSNSSNNEQ LFLVSELTSD
LYETENVSRR LIQTGTKEDI VLYQAQLDSI KMNLVELDEQ YAENQLHTEL DSIYKLLDLK
TENLEALINL REKERNTNYY KQVMEELNRV NESFESNQGY DDRFNDLEPY QKRVLVKWLE
YARADNARSL TNQTADSLVN SVKKVLNDFQ KANIKFRQTI IEKENDLLDN DMVLNQQLRK
ILANIEKDER EASLERTEKA QQTLEDTVSI IMVSGIVCVI VILLFLMLII RDVRRSQQYR
IELEEAKNFA ETLLKRREQL MAAITHDLRS PLNTVIGYSE LMNKTQLGNK QRHYLSQINK
SSDFILHLVN DLLDLSKLEA GKMLVENLPF NPKKLISDTV QNNIPANLNK DLEVIIDISE
EADGQYSSDP FRIKQIIANL VTNACKFTEK GNIIVSAEIE TKTKDIQYLI IKVKDTGIGI
SKEKQEVIFE EFSQENSGIE KKYGGTGLGL TITKSLTSLL KGEISLQSEQ GKGSEFTITI
PVQKSKNQKK PVPENPHPPT EKTDSLDLGN KKVLVVDDEP AQLALTLEFL KNHLLKFDTA
ENGKKALELL GKNQYDLILT DIQMPIMDGF QLMNAIKKDK NLNKTPVIAL SGRTDMKDEV
YTLTGFTAKL TKPFKPKDLL LSISEVFNVE TKTEEKPLIP KNDFTPKHNE FYNLEDIYMF
SGQDKEAMHI IIKAFLESSQ ENIAKIKFHK KDKNYDAIGQ IAHKMLPMFK QMRITPVIPV
LERLEKKVEV CDTEIDELIQ QLQTVLRELE NEVIV
//
