ID A0A245ZIH7_9SPHN Unreviewed; 827 AA.
AC A0A245ZIH7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=evgS {ECO:0000313|EMBL:OWK29534.1};
GN ORFNames=SPDO_25260 {ECO:0000313|EMBL:OWK29534.1};
OS Sphingomonas dokdonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=344880 {ECO:0000313|EMBL:OWK29534.1, ECO:0000313|Proteomes:UP000197290};
RN [1] {ECO:0000313|EMBL:OWK29534.1, ECO:0000313|Proteomes:UP000197290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21029 {ECO:0000313|EMBL:OWK29534.1,
RC ECO:0000313|Proteomes:UP000197290};
RA Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Sphingomonas dokdonensis DSM 21029.";
RL Submitted (MAR-2017) 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:OWK29534.1}.
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DR EMBL; NBBI01000004; OWK29534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A245ZIH7; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000197290; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 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; IPR007891; CHASE3.
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; IPR013767; PAS_fold.
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; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:OWK29534.1};
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 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..266
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 354..571
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 584..699
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 708..818
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 633
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 756
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 827 AA; 90456 MW; 2086931916EAB2E4 CRC64;
MTLAPPRKPS AWPFVAVALL IPIVLAATLF WIQGEYSRWE TLRLGAQQSY SRRSHLVDLL
STMRAAETSE RGYALGGEDQ LRTRYVAAEG AVRRLLRDLF RAYRQERSPP QIGELSRIAD
AKFAEMDEVI HLYDRLGAAA ARRRINEGDG QRLMAQFEQL VGNVFRREIQ VGDQRVQAFR
ARAAWIEWMM WVIAAIASVA LTVILTQLWR QRRAKYEAAL AAYEAAERNQ TILNATADPI
VIINASGTIE TINAAVTRVL GYTPEDAERR DVAMLSDIAP GVGNFIERIG FADGSLRTSF
LQEQPIRTRF GETILFDVAL GVMRLPDGDH IVASLRDTTE RQRLDRLKDE LISTISHELR
TPLTSVIGAL SLLRADAAGA LPEEAQELVQ IAESNGQRLI RLINDMLDID RIEAGNFRLA
TAPLDLRDVV RRACNDHAVL ATSHAVTLDC QLPNELLMVE GDEARLLQVL ANLLSNAVKF
SPEGGKVTVC ARHDARALQV EVADEGHGIA EEFRSRIFGR FERAPRSEGW SGTGLGLAIA
RDIVTRHGGD IWFEDRPTGG TRFVFSLPAI DAADSAGADA DRRQVLICEA DARLGQELQT
LVEAEGLTGR VVTSAAAARD ALADGGYDLL ILDMALDDPD ALTFARDVRR AVAPGALSII
LVSPDGNADA AARFSLDLVD WMDKPVHPAR LKAALAAAMP ANKADMPIVL HLDDDQDTLD
VTARTLSGTA RILKARSLAE ARAILRDQTP DLAILDYHLA SGTGLDLLPD LTTTCGLAIP
AIVYSAHDVL LDPEALVDAV VVKSRHSAVD LKATIRRVLS VRHERAG
//
