ID A0A426GH96_9CAUL Unreviewed; 1123 AA.
AC A0A426GH96;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EIK80_15855 {ECO:0000313|EMBL:RRN63587.1};
OS Caulobacter sp. 602-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN63587.1, ECO:0000313|Proteomes:UP000268773};
RN [1] {ECO:0000313|EMBL:RRN63587.1, ECO:0000313|Proteomes:UP000268773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=602-1 {ECO:0000313|EMBL:RRN63587.1,
RC ECO:0000313|Proteomes:UP000268773};
RA Gao J., Sun J.;
RT "The genome of Caulobacter sp 602-1.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential protein that is involved in the control of cell
CC division, probably through the regulation of ctrA. Its phosphorylation
CC status is regulated by PdhS. {ECO:0000256|ARBA:ARBA00037447}.
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 -!- SUBUNIT: Interacts with DivL, PleC, DivJ and PdhS.
CC {ECO:0000256|ARBA:ARBA00038776}.
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:RRN63587.1}.
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; RRYI01000005; RRN63587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426GH96; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000268773; Unassembled WGS sequence.
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; cd00156; REC; 2.
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; SM00065; GAF; 1.
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};
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}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 459..679
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 730..843
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 852..969
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 998..1121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 682..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..442
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 687..701
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 779
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 901
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1054
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1123 AA; 123051 MW; DE1CE5BCF7D6B621 CRC64;
MGLALAFFLI SGTIAYRNIE TLRINSEKIW HTHEVLIALD DLLSTTQDAE TGQRGYLLTG
NDRYLAPYQR AVTDVATRTE AVGSLTKDNP IQQANHAQLR RHIDAKLSEL AETVALRGSQ
GPQAALAVVN TDRGKAEMDA IRQQIDVMRA EENRLRDIRL TEMDIAHRTA LISSVLSAVL
GAALTFAVFA LIRRSSQARA RQQWLQAGQV GLSEVMMGDK TVEELSDSIL HFLSRYVGFQ
AGALFKGENG RFYRAAALGI PADADTPLHF NIKEGLLGKV AAEGHATVVR DVPDGYLTIG
SALGHDKPKH LVLVPTHADD IVNAVIELGF LHAVDDQVLE LLNQVSTSIG VSLRSARYRS
QLQSALEETQ RQSEELQVQS EELRVSNEEL EEQGRALKES QIRLEQQQVE LEQTNSQLEE
QAQTLEAQRD ELERTGAAVQ LKARELAQAS QYKSDFLANM SHELRTPLNS LLILSKLLSD
NPAGNLSSEQ VKFAQTIESS GNDLLTLIND ILDLSKIEAG HIEVRPESVP LQRLTNDLRS
LFQPLADERQ LGFEIKVATD TPTLLETDRQ RLEQILKNLL SNAFKFTQAG RVTLAITPTG
DNEIAFAVTD TGIGVAREQQ ESIFEAFRQA DGTISRKYGG TGLGLSISRE LSRLLGGKIA
LESTPGEGST FTVTIPRSYD PARVAPRPEP SASPAPAPAV PAAPARARAA APMTRTIEDD
RDQLANGRRV LLVIEDDDKF ASIVRDLSRE LGFQCLVAGT AEDALKLARQ FKPSAVVLDV
GLPDESGLMV LDRLKRDDAT RHIPIHVISG ADHSQTALSL GAIGYMVKPV KRDDLAQVLT
NLQSKLSSTV RRVLIVEDDD VQRDAVGKLL SSGDVETVGV GTAAECLEAL KTQTFDCMVL
DLSLPDASGF SLLETLSQDG DHAFPPVIVY TGHDLSADDE QRLRRYSSSI IIKGAKSPER
LLDEVSLFLH QVVSELPPEQ QKMIKKARNR DAVLEGRRVL IVEDDIRNVY SLTNVLEPRG
AVVEIARNGK EAIEALDRSA QGDPANAIDL VLMDVMMPVK DGLTATREIR EDARWAKLPI
LMLTAKAMPD DQARCIAAGA SDYMAKPIDV DKLLSLVRVW MPR
//
