ID H6R5W2_NOCCG Unreviewed; 865 AA.
AC H6R5W2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=kdpD {ECO:0000313|EMBL:CCF64652.1};
GN OrderedLocusNames=NOCYR_3889 {ECO:0000313|EMBL:CCF64652.1};
OS Nocardia cyriacigeorgica (strain GUH-2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF64652.1, ECO:0000313|Proteomes:UP000008190};
RN [1] {ECO:0000313|EMBL:CCF64652.1, ECO:0000313|Proteomes:UP000008190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF64652.1,
RC ECO:0000313|Proteomes:UP000008190};
RX PubMed=22461543; DOI=10.1128/JB.00161-12;
RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA Richard Y., Cournoyer B., Blaha D.;
RT "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT cyriacigeorgica GUH-2.";
RL J. Bacteriol. 194:2098-2099(2012).
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; FO082843; CCF64652.1; -; Genomic_DNA.
DR RefSeq; WP_014352107.1; NC_016887.1.
DR AlphaFoldDB; H6R5W2; -.
DR STRING; 1127134.NOCYR_3889; -.
DR KEGG; ncy:NOCYR_3889; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_1_11; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000008190; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR InterPro; IPR002035; VWF_A.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 371..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..314
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 607..826
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 805..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 91938 MW; 5489007854251951 CRC64;
MKRGHLRIYL GAAPGVGKTY AMLGEAHRRL ERGRDVVAAV VETHGRAKTA ALLDGIERIP
PKVIEYRGTA FQELDVAAVL RREPAVVLVD ELAHTNAPGS KNEKRWQDIE ELLDAGIDVI
STVNVQHLES LNDVVEQITG IQQRETVPDA VVRAAEQIEL VDITPEALRR RMSHGNVYAA
DKVDAALRNY FRPGNLTALR ELALLWLADQ VDAALAKYRA DHRITDLWEA RERVVVAVTG
GPESETIVRR ARRIATKSSA ELVVVHVVRG DGLAGVSTAR LTRLRELAAG LDASLHTVTG
EDVPAALLEF AREVNATQLV LGTSRRSRWA RIFDEGIGSA VVQQSGKIDV HMVTHEEANR
RRSWPSLRRP VWAWVAALVV PVLVCAIGAW FLDGALELGG LSAMFFVAVV LVSLLGGVLP
AAISALLSGV LLNWFFAEPR YSLTVAEPDS IFTIAVLLIV AVAMAALVDR AAARSRQARK
ASRQAELLTV FAGAVLHGAD LPKLLEQVRE TYGMRAVALV AGEDVLAAVG AEPPCRPGDA
DTTIEAGDTV HRLLLAGHPL DPGDRPVLTA VANQAVGLVR QARLAEEAGA AAALLEADRL
RRALLSAVSH DLRTPLAGAK AAVSSLRSDD VEFSPEDTAE LLETVEESVD QLTALVGNLL
DSSRLAVGVV SPQLRQVYLD EVVHRALVGV GMGARGLRRA AMDRVEVDVD ALSVRADGGL
LERVLANLID NALRHSTPGT PIRITAERDG GKVAIAVVDI GPGIPAGAEE QLFEPFQRLG
DRDNSTGVGL GLSVVRGFVE AMGGTVHAEP TPGGGLTMLV ELPAGADAAP PRDSDESGEG
PATMDSAGSS RGDDPAQGPD RAGVT
//
