ID A0A344PJZ8_9RHOB Unreviewed; 885 AA.
AC A0A344PJZ8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DRW48_08390 {ECO:0000313|EMBL:AXC49703.1};
OS Paracoccus suum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=2259340 {ECO:0000313|EMBL:AXC49703.1, ECO:0000313|Proteomes:UP000252023};
RN [1] {ECO:0000313|Proteomes:UP000252023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2-6 {ECO:0000313|Proteomes:UP000252023};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of Paracoccus sp. SC2-6.";
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};
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DR EMBL; CP030918; AXC49703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344PJZ8; -.
DR KEGG; pars:DRW48_08390; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000252023; Chromosome.
DR GO; GO:0016020; C: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; 3.30.450.40; -; 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; 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; 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 PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 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; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AXC49703.1};
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:UP000252023};
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 389..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 659..876
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 885 AA; 96396 MW; 63986A44B7477598 CRC64;
MLESAQRETR GHLKIFLGAA PGVGKTYEML MSGRAQRADG VDVVIGVVET HGRAETEALV
DGFEIVPRRT VPYRGHVLDE MNIDAILARK PALVLVDELA HTNAPGSRHP KRYLDVEELL
ANGIDVYSTL NIQHVESLND VVAQITRIRV RETVPDSIID RADDIEIIDI TPGDLIKRLN
EGKVYLPKTA KRATQNYFSP SNLTALRELA LRRTAQRVDD QLVTHMQAHA IAGPWSAGER
VLVCINERPG AMALVRYGRR QADRLRAPWA AVHVETSKDG RLSEQQKDKI ASALRLAEQL
GAEAVTLPGE NVAQEILAYA STNNYAHVIV GMPTSPRWRE IFAGSVSHDL IRAKTDVSVH
VISPGNGEET RSPATVSARP KRRIDFGHYL WSSLYVAMAL GIGTALSRFL DVRNIALVFL
MAVLASAMGG GLWPALFASV LGALVFNFFF LEPRYTLDIG DPESVVAFAF FLGVAVIASN
LAGRVQRQAV TARQRAKTTE GLYLFSKKLA GAGTLGDVLW ATVYQIASML QVRVVALLPE
NGRIAVQAGF PPDDTLDDAD IAAAQWAWEH DKPAGRGADT LPGAKRLYLP LKTGRTRVGV
IGLDNDKQGP VLTPLEQRLF DSLADQAALA IERIQLVADV DNARLAVEAD KLRSALLTSL
SHDLKTPLAS ILGSAGALRD YSTSLTDSGR VELLTTIVEE AERLNRFIAN LLDMTRLESG
AAAVSLTPLF IGDSVGSALR RAEKILTLHR VDLAVPPDLP MVRLDPVLFE QVLFNLLDNA
RKYAPSGSRI ALRAWADESH VTLQVVDEGP GIPPDDLTRI FDSFYRVRKK DHVQAGTGLG
LSICKGFVEA MGGTIFATNR ADRPGAIFTL RFPIGPEPST LEGRI
//
