ID A0A239FPK8_9RHOB Unreviewed; 790 AA.
AC A0A239FPK8;
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=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421757_102781 {ECO:0000313|EMBL:SNS58857.1};
OS Tropicimonas sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNS58857.1, ECO:0000313|Proteomes:UP000198426};
RN [1] {ECO:0000313|EMBL:SNS58857.1, ECO:0000313|Proteomes:UP000198426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29339 {ECO:0000313|EMBL:SNS58857.1,
RC ECO:0000313|Proteomes:UP000198426};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZOY01000002; SNS58857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239FPK8; -.
DR Proteomes; UP000198426; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198426}.
FT DOMAIN 294..515
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 533..651
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 687..781
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 582
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 726
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 790 AA; 85133 MW; 54F19A81E6484FEE CRC64;
MRKLEALIQE NEDWLVDRVV YYAVSEGFSD YTSTLREAWR ASICGLSTPI LGAIAAAGDT
SNSRKGFGKA RETIVAFGVD QALKHRARGI QLTDFLGLLK YYRRAYLDLI DEHPMPESDA
RRLRGWILDF FDQVEIGLCG EWISASDAQR LRDLQDRAKS LTNEKNKYLT IFESIREPVI
LLDANHHPTH LNHAAHLLFC GEVTPGASYY GASNSPLLNA QITSMLEGAT DGGHDAVIKT
LSGPREFNVN TQKMLDVSHK FDGTVIILND VSEYKRALRR AEAADQAKST FLAAMSHEIR
TPIAGVLGLA RLLRDTELTP GQSRHVEGIL SSGELLAGVV SDILDFSQAE IGGRKPVPEN
FDVAGVVRQI FMVVERAATD KGLRLVSQIA PETPAQLRGD TSMIRQVLLN LAHNAVKFTE
QGEITVRVAP LTRDDGSERI RFEVRDTGVG LPDGPCEWLF DPFTQHDRDR ASLKGGVGLG
LAICKKIVSS LGGEIRCFAN SPGGSVFQVD LPLEPGVSVV EPAGNKPHPV GAKVLVVDDD
DVNRAVAEGF LSKLGHVAVS VPSAADALEM LSSQPFDLVL SDNRMPDITG LELLTRIRAL
RTGPNREVPV VIVTASVGDV KAGAAGAMAP DGVLGKPYDM DDLARELGTL LSDRGIAPAH
GNASPRTTPP PSDADLTTLL QHMSHLGPER SQRILKAFAD TAPARLEAID KGVSERDWDE
VSAAAHALAG ASGILGLESI SHCAREIVSK AEKGDRSRIA EDLSHLKQQV VDVQGKLLAL
AEGASTSPNG
//
