ID A5CDH2_ORITB Unreviewed; 1145 AA.
AC A5CDH2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=OTBS_0841 {ECO:0000313|EMBL:CAM79907.1};
OS Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM79907.1, ECO:0000313|Proteomes:UP000001565};
RN [1] {ECO:0000313|EMBL:CAM79907.1, ECO:0000313|Proteomes:UP000001565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boryong {ECO:0000313|EMBL:CAM79907.1,
RC ECO:0000313|Proteomes:UP000001565};
RX PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT "The Orientia tsutsugamushi genome reveals massive proliferation of
RT conjugative type IV secretion system and host-cell interaction genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000256|ARBA:ARBA00006434}.
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DR EMBL; AM494475; CAM79907.1; -; Genomic_DNA.
DR RefSeq; WP_011944672.1; NC_009488.1.
DR AlphaFoldDB; A5CDH2; -.
DR KEGG; ots:OTBS_0841; -.
DR eggNOG; COG0591; Bacteria.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_010010_0_0_5; -.
DR Proteomes; UP000001565; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd10322; SLC5sbd; 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; 1.20.1730.10; Sodium/glucose cotransporter; 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; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00474; SSF; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:CAM79907.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001565};
KW Transferase {ECO:0000313|EMBL:CAM79907.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 732..960
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1013..1132
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1064
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1145 AA; 128686 MW; 6984D0CF8F5EAFC3 CRC64;
MPALNIDIIL VGLFLIANLA IGLWYGKEVK SVRDYAISGR NFSTAALTAT LIATWIGGST
FSFKLSQIYT LGILAFLPVI GQVLNLLITA YILIPRMQEF LGKLSVADVM GDLYGTHIRT
ITAICSIIRA STRIAMQIKV FSTIFYHFLG VDSVYATLIS SMIVIIYSAF GGIRAVVFTD
VFQSLAFGAF IPTLAILIWG MFGSWESIVN TLTTNPIFDP KILLDYHNIN TLKYYGMFVY
FVLPEINPAM FHRVLIARST VQAATAFKVM LLVHLSFCIF VGFIGLTLLS AHQNIEANNL
VPYIIDSYAY PGFKGLVVIG ISAMIMSTAD SWINSASVIF VNDLCKPLGL FQNDAKLEFK
AVRIFAIFIG GIGLYIALSQ KNLLDILLFG ASFSTAIVGI PLMFTILGFR TTTRVILSGM
IAGIATVFIW NRYFDAVLPI GDVIPTAIVN FSVMMIMHYC LGEPGGWVGP SDRRPLNVLK
EKRKQQINSI SSFFKSLSHS FSWDNICAYC NNETFRGRHY YIEYSVITAA SLMVMSLCGQ
VEHNIASAWL VTKVSVILLG LVMTTALLYN NKWNADFRTK YLGLIWHITI FYTLVFSNTL
LTMIGGSSPI LLMCFISNLV VAGILLQWHT ALFMILLGVP VGARVFNILA SWRGYLADYN
EVDNNLGMYV IWALALLTAI LLFIRLRQNQ FVDNTRSMLE LKNDVDVLNL RLNTKSQKME
ILLNTEKHIL NNLSHEIKSP LSVVRTTINL LSKFLPKYYK DTQMILKEKE RVLTMVTLAN
SGIERLVAYS NNLFDLSKFA QGQMIFDIEL NNFQLMLKEI IAECNKVNVA EKHIISLNYV
PQAETMFEFD HTRIKTVMLN LISNAIQYSQ SGLILITVKP YRSGVEVSIE DEGVGIPENE
LEAIFVPFEE SSRTKSKACG RGLGLTLAKE IILAHHGEIW AENRPNNRGS KFTFRLPLRQ
PEGGFNKAVY SKSEVFGKIY KDRIAKLLKG FGYECNSINS LKELENHIRV NKSILIVDDD
QNILDAISLD IYAEQYTPEP VNNAFEAVKL IKENPLQYSL VLLDMVMPEK SGEQVVQEIY
TVTKMYGIPI IIISGYSQTY ETKNLLYSMG VVAFIEKPYT YNQLRNVINH YLKQTIIPLP
YSYLP
//
