ID C6Y0P8_PEDHD Unreviewed; 1161 AA.
AC C6Y0P8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Phep_0587 {ECO:0000313|EMBL:ACU02809.1};
OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU02809.1, ECO:0000313|Proteomes:UP000000852};
RN [1] {ECO:0000313|EMBL:ACU02809.1, ECO:0000313|Proteomes:UP000000852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC {ECO:0000313|Proteomes:UP000000852};
RX PubMed=21304637; DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT 3).";
RL Stand. Genomic Sci. 1:54-62(2009).
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; CP001681; ACU02809.1; -; Genomic_DNA.
DR RefSeq; WP_012780762.1; NZ_AQGK01000003.1.
DR AlphaFoldDB; C6Y0P8; -.
DR STRING; 485917.Phep_0587; -.
DR KEGG; phe:Phep_0587; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_000445_127_1_10; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000000852; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; cd19410; HK9-like_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ACU02809.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000852};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACU02809.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 495..730
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 768..882
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 892..1009
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1043..1160
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1013..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..478
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 817
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 941
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1093
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1161 AA; 130121 MW; 883C17EC44B4830C CRC64;
MFKLTFKQQV LTGFTVSLLF VLVSAITSYF SIDKLNSDTK WQSHTYDVIS LLKDVEGQVL
NSETGVRGFI LAGKPQYLAP YKKNSVKILP TIQELKRTLD QDTAQEILID SLDYYAHEKV
DEMKAVLQLY DAKGKDAAAF RVMAGQGQFF KNKILELSGK IISKEKQLLQ KRKADIIKSS
KQSEFVVLLS AFIIFCLILF LFSYIRRTFD QQKETESQIR DSNLQLERIS AENEQKNWLL
LGTTAINEAM RGEQEIEELA SNIITQICNY IHAPIGAFFL ANPSKKTLRF EGGYAYQHTK
SIRQEYHFGE GFVGQVAVEK KRKLLEPVPA GYIKVNSGLG EAPPACIYLM PIVFEDQTLA
VIELGLNQQP NDSISLFLQA ITESIGVGVN SAVARVKLRA LFEQTQQQAE ELESQQEELR
TTNEELVYKS EQLQASEEEL RVQQEELRQT NSELEEKAQQ LEERNIAVNQ AKEAMSLKAE
ELEISSKYKS EFLANMSHEL RTPLNSILIL ARILKENRPE NLNEDQIKYA GVIHNAGTDL
LTLINDILDL SKIESGKLDL SILPLKPLVI KQDMEALFNE LAKSKKISFH TVLDKELPAT
LLTDQSRLEQ IVKNLLSNAF KFTPEHGEIT MTISKASAGT LFFSRQLKTT TEDIIAISVK
DSGIGIPADK QKLIFEAFQQ ADGSTSRKYG GTGLGLSISK ELAHILGGEI QVNSKQGEGS
TFTLYLPKNN ATAPENQENI SEIEEATIIP LVPDPVLMPV NRHKDAQKLL IVEDDLVFAD
VLNDYAIEKG FKPILAHSGD VALEMAFSEL PDAIVLDIML PVMDGWTILK KLKADPRTKH
IPVHMMSAGN EKAGKAKKEG AIGFLKKPIE KEQLDEAFDL LSAAHLKYNL NKVLLIEDQE
LHSKLLAQQL TEKGVDVKQA FTGKEALVLL DEQTFDCIIL DLKLPDISGF DLLDSIKSQE
KLVQVPVIIN TAMELDQDKM AHIMQYTEAM VLKSNKSNDR LIDEVSLFMN KLKKEGPPPT
SANGRPPKNK ASSTMEKVLK DKTILITDDD MRNIFALSSA LQAYDLKIVI ANNGREAISK
LEETEPIDLV LMDIMMPEMD GYEAMRTIRS KKEFAKLPII ALTAKAMKND KEKCIEAGAN
DYISKPVDMD KLLSMLRVWL S
//
