ID A0A425Y8K9_9BACT Unreviewed; 950 AA.
AC A0A425Y8K9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DWB61_02250 {ECO:0000313|EMBL:RRG24851.1};
OS Ancylomarina euxinus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2283627 {ECO:0000313|EMBL:RRG24851.1, ECO:0000313|Proteomes:UP000285794};
RN [1] {ECO:0000313|EMBL:RRG24851.1, ECO:0000313|Proteomes:UP000285794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1P {ECO:0000313|EMBL:RRG24851.1,
RC ECO:0000313|Proteomes:UP000285794};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Ancylomarina sp. M1P.";
RL Submitted (JUL-2018) 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:RRG24851.1}.
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; QQWG01000001; RRG24851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A425Y8K9; -.
DR OrthoDB; 9796457at2; -.
DR Proteomes; UP000285794; 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; 2.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 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; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00062; PBPb; 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 SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 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}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 316..389
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 394..446
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 587..811
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 832..947
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 882
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 950 AA; 108421 MW; 07948FF8DB8CDB17 CRC64;
MYLHTINPRR SFSIYLFTIT LLLIVLSCQR SNEPFITHDE RMWLDKNEGK IEILFGYQEP
PLAFHNENGD YVGLLIDYQK EIENSLGFDF KFRNFDTWEE LITYSQTAHN YIIVGCASTN
KREEYLSFTN SIVKIPYVII SQKNSNITSM SSLADKNICT VSNYAVNDYI AQYYPNITPI
SFKNHIECIR AVSTGDCDAM VVSQMTVTHI IDTELISNLK ISDGSGYMNR LAVAISKDDP
TLFKIIDKII DNIPLNRQKE FHQKWIHSRP NKFSKKTWLT IISILSIFIL AFIILWLWLI
SVKKLVAKQT RQIRENEENL RITLNSIGDA LIVTDVEGKI TRMNPVAQKL TGWHFNEAKD
QSLERVFKIV NSTTKERVED PVKKVLNCGQ IIGLANHTVL ISKDGREFQI ADSGAPIKDE
TGNISGVVLV FRDVTEEYKM QTALEENEAK YRSLIENSND AIYLLYNNHF ELINKRFEEI
LGYTSQEMKH INLYNLIATE SLEMMNIRIQ ENDKSKLSQK FEFVGIAKSG KKIPIEVSSS
FIPYKDGIAN QGIIRDISQN KKHESDLIKA KEIAEESDRL KSVFLATMSH ELRTPLNAVI
GFSDLIKADL SLEEIIYYSE IINMSGKHLL GVIEDVFDIS LIETGDIKIE NEPLSINTLL
NEVYEIIKNE QTLQNKEHVD LILNNSLENQ DTILFSDQKR IKQNLINLLK NALKFTEKGR
ITFGCNLHKE NQQEFIQFFV KDTGIGIPPN KQKLIFEVFR QADDSHTRIY GGSGLGLTIC
KKLTNLMGGD IWVESKEGDG ANFIFTIPFS DNYDSNIDSS KTSPILNFNN KTVLIAEDDE
TCFSFLEALL SPKGMNCVRV NNGEEAVEYC QNKNKVDLLL MDINMPKMNG YIATEKIKKI
RPKIPIIAQT AFAIEGDKEK ALAAGCDYYI SKPINKNDLF DKILLSFDIN
//
