PDHS_BRUSU
ID PDHS_BRUSU Reviewed; 1035 AA.
AC Q8FZ86; G0K6E3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Cell-division control histidine kinase PdhS;
DE EC=2.7.13.3;
GN Name=pdhS; OrderedLocusNames=BR1606, BS1330_I1600;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- FUNCTION: Functions as a polar differentiation marker. Essential
CC protein that, by localizing in the old pole of dividing cells, controls
CC cell division and maturation, probably through control of DivK
CC phosphorylation status and cellular distribution, which in turn
CC regulates CtrA, a transcriptional regulator of the minB operon. The
CC asymmetrical localization of this protein is probably required for
CC cells to enter a new division cycle (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Interacts with DivK. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes at the
CC old pole of dividing cells. Colocalizes with DivK (By similarity).
CC {ECO:0000250}.
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DR EMBL; AE014291; AAN30511.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18927.1; -; Genomic_DNA.
DR RefSeq; WP_006190713.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8FZ86; -.
DR SMR; Q8FZ86; -.
DR EnsemblBacteria; AEM18927; AEM18927; BS1330_I1600.
DR GeneID; 45052594; -.
DR KEGG; bms:BR1606; -.
DR KEGG; bsi:BS1330_I1600; -.
DR PATRIC; fig|204722.21.peg.3518; -.
DR HOGENOM; CLU_000445_23_0_5; -.
DR OMA; NAHKTDF; -.
DR PhylomeDB; Q8FZ86; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Transferase.
FT CHAIN 1..1035
FT /note="Cell-division control histidine kinase PdhS"
FT /id="PRO_0000361904"
FT DOMAIN 659..730
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 802..1031
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..613
FT /note="Important for polar localization"
FT /evidence="ECO:0000250"
FT REGION 500..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..1035
FT /note="Interaction with DivK"
FT /evidence="ECO:0000250"
FT COMPBIAS 504..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 805
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 1035 AA; 111740 MW; 2D65B348A1433D40 CRC64;
MSGSYPFIDI AALDSVREGF ARGDAQLVLA HDLSTVLWVN GPGAKLFGYN RVEDLIEGQL
DLPVATRRQI AAFSSENTSA PSAVAVRLGG GLRSELTHLH VSNIKLPDGV AALLVATQMP
DNSAEAAISG LGDDSTHIAL VDAVGKVVAA SPRFALLDIS ASTLEDLIVE AGDATDRIVK
RRIRTGSHSV PGAIARLTDT PALHLLCIVG DAPAQFQTAA EAVPLPDNAE AVLEEILPEQ
GDAPAQQAQK THAEQPRPKT FAFDHDAPPA RFIWKVGPDG TFSEISPDLA AVVGPNSADI
VGRRFSDVAN VFGFYTDGSI AALLLERDTW SGKRLLWPVE GTRLRVPVEL AALPVYSRDR
EFLGFRGFGI VRPAEAEADP EEIGLALAGG IPQNRKPRKE PAETARMVGE DDVLALSEEV
ANDDQPAAVL PKPPLDITPT PGRRDSDKVI SLLNSCAQEK VAADQAKFLK EKERATRPEG
GLTKTERNAF REIAERLRKQ GLANTRAESE TPVSETSSIE PVEPTPPVKT RSEPIQPDET
ALLANLPVPV IIHSGDAIHY VNQALLDITG YESLDDIRSA GGVDVLFNSE SDDGETRQSM
VLRHADGSEE PVDAHLNAIA WRGGRALMLS LMPVTAADLP APAELPAAND EEKQALEAHV
EELKTILDTA TDGVVLIDPE GRIRSMNHSA SALFGYERDE AEGKFFSMLF AIESQRAAMD
YLHGLSGNGV LSVLNDGREV IGREAKGGFI PLFMTIGKLP HTRGFCAVLR DITQWKRTEE
ELTNARKEAE RASNQKTEFL ARISHEIRTP LNAIIGFSEL MADEKFGPIG NDRYRDYLRD
INRSGNHVLA LVNDLLDISK IEAGALDMQF EAVSLNDAIG EAIALMQPQA NRERVIIRSS
FQSNLPDIVA DSRSIKQVAL NLLSNAVRFT APGGQVIVST SYELNGDVVM RVRDTGIGMS
KSEVEQALKP FRQINALEGR KAESAKDWRN EGTGLGLPLT KAMVEANRAQ FAIDSNPGQG
TVVEIVFPPT RVLAD
