ID   Q2W139_MAGSA            Unreviewed;       625 AA.
AC   Q2W139;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
GN   OrderedLocusNames=amb3632 {ECO:0000313|EMBL:BAE52436.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE52436.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE52436.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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}.
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DR   EMBL; AP007255; BAE52436.1; -; Genomic_DNA.
DR   RefSeq; WP_011385990.1; NC_007626.1.
DR   AlphaFoldDB; Q2W139; -.
DR   STRING; 342108.amb3632; -.
DR   KEGG; mag:amb3632; -.
DR   HOGENOM; CLU_437309_0_0_5; -.
DR   OrthoDB; 9811749at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd16936; HATPase_RsbW-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR036890; HATPase_C_sf.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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:UP000007058}.
FT   DOMAIN          251..368
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         301
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   625 AA;  66800 MW;  C2BC374396AE1E35 CRC64;
     MTIVAVMEGA CPRLEEQIRL LGWPRVAAPG EGGRNDERAV MVREAFTPQA LIDCLSPPWI
     GGIEAAGSGG HPVGSCFRRH LAEGGLGLSL RSDTAYGADI AVPFADALAT RLLAPGTDSF
     DLGFVVQELV SNALLHGNLE VGGIDCEGGG GLEGFGERIE AALGDPGRAG RRVQISASVV
     GDRLEVAVED DGPGFDHVDG HANPRRPHGL ALLESMVSDL HTEEGGRRAI ATMVIPTRQL
     RAEPLGLDDV RVLVVDDNLM NRVLMETLLR RMGVGQVETV ESGEKGLAAI EREKPDLVLL
     DVMMPGMDGF EMCRRLRRLH PLTELPVIFV TALDGPADRN ACFAVGGSDM VAKPIDANEV
     AARVGVHLRL GQAMDRLTAY QDRVHEELRA ARGAQAALMP TSAELSSIRI RQGLVVDGRI
     ESSSELGGDF WTVLPAGPNQ MFLLVADFTG HGPVAAFNVF RLHLLLSRLP RRMPTPSALL
     EYLNLELKAV LRSGQFAAAF AALIDVEEGV MTYAGAASPP AVLVVDGEVR FLDADGPPLG
     AFVDAEYEES RIALPRGAAL LAYSDALVES QGSDGRMACD QETLREWVLG AQPGHSLADE
     VLARFREKVP GEPPDDLTLV SIRRP
//