ID W9HG15_9PROT Unreviewed; 402 AA.
AC W9HG15;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
GN ORFNames=N825_01745 {ECO:0000313|EMBL:EWY42853.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY42853.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY42853.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY42853.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) 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 -!- 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:EWY42853.1}.
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DR EMBL; AVFL01000001; EWY42853.1; -; Genomic_DNA.
DR RefSeq; WP_051511393.1; NZ_AVFL01000001.1.
DR AlphaFoldDB; W9HG15; -.
DR STRING; 1385369.N825_01745; -.
DR OrthoDB; 9793549at2; -.
DR Proteomes; UP000019486; Unassembled WGS sequence.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_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; PF00072; Response_reg; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 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:UP000019486}.
FT DOMAIN 12..129
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 402 AA; 41668 MW; 19AD6909C480E04F CRC64;
MAQPIAATRP ERLLVVEDDE FSQQLIELYL RKAGFTELTV ANDGRQALDL AKANTFDLIL
LDLGLPRIGG TEVVRRLKKE GLLANTPVVV ISAITNMEDT IQCIEMGASD YLAKPFNVMQ
LQQRVDACLE RQRLRRESAA TKRRDALDES AALGLRAALA LPAFPRSGPG FPAEGAVLSE
ASRGGGQGRD FHDVFPVLGG GTGFVVGTVA GTGIAALLTV ARVRALVRVL ADRFDPSGGA
PLDPAALITQ IGAELASDPA EGSEDGRSIA LFIGVLQAGG PLRHANAGMP TPVVLSQMLG
VLPLAGKRGP PLTGDASFEG PVGGQVSLQP GDGLVVHTRG LVEATDAGGG AYGEQRLKVA
LDALIAAPAA LISSTLREDA AGFAGGVPFK DDVTIVALRL VA
//
