PDHS_BRUO2
ID PDHS_BRUO2 Reviewed; 1035 AA.
AC A5VRX4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Cell-division control histidine kinase PdhS;
DE EC=2.7.13.3;
GN Name=pdhS; OrderedLocusNames=BOV_1549;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(2009).
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; CP000708; ABQ60845.1; -; Genomic_DNA.
DR RefSeq; WP_006013398.1; NC_009505.1.
DR AlphaFoldDB; A5VRX4; -.
DR SMR; A5VRX4; -.
DR EnsemblBacteria; ABQ60845; ABQ60845; BOV_1549.
DR GeneID; 45124921; -.
DR KEGG; bov:BOV_1549; -.
DR HOGENOM; CLU_000445_23_0_5; -.
DR OMA; NAHKTDF; -.
DR PhylomeDB; A5VRX4; -.
DR Proteomes; UP000006383; 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_0000361903"
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; 111924 MW; 5D7CF8612E37833D CRC64;
MSGSYPFIDI AALDSVREGF ARGDAQLVLA HDLSTVLWVN GPGAKLFGYN RVEDLIEGQL
DLPVATRRQI AAFSSENTSA PSAVAVRLGG GLRSELTHLH VSNIKLPDGV AALLVATQMP
DNSAEAAISG LGDDSTHIAL VDAVGKVVAA SLRFALLDIS ASTLEDLIVE AGDATDRIVK
RRIRTGSHSV PGAIARLTDT PALHLLCIVG DAPAQFQTAA EAVPLPDNAE AVLEEILPEQ
GDAPAQQAQK THAEQPRPKT FAFDHDAPPA RFIWKVGPDG TFSEISPDLA AVVGPNSADM
VGRRFSDVAN VFGFDTDGSI 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 APGRQVIVST SYELNGDVVM RVRDTGIGMS
KSEVEQALKP FRQINALERR KAESAKDWRN EGTGLGLPLT KAMVEANRAQ FAIDSNPGQG
TVVEIVFPPT RVLAD
