PDHS_BRUA4
ID PDHS_BRUA4 Reviewed; 1055 AA.
AC A6X5X4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cell-division control histidine kinase PdhS;
DE EC=2.7.13.3;
GN Name=pdhS; OrderedLocusNames=Oant_3923;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(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; CP000759; ABS16628.1; -; Genomic_DNA.
DR RefSeq; WP_012093273.1; NC_009668.1.
DR AlphaFoldDB; A6X5X4; -.
DR SMR; A6X5X4; -.
DR STRING; 439375.Oant_3923; -.
DR PRIDE; A6X5X4; -.
DR EnsemblBacteria; ABS16628; ABS16628; Oant_3923.
DR KEGG; oan:Oant_3923; -.
DR PATRIC; fig|439375.7.peg.4095; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_23_0_5; -.
DR OMA; NAHKTDF; -.
DR OrthoDB; 1755994at2; -.
DR PhylomeDB; A6X5X4; -.
DR Proteomes; UP000002301; Chromosome 2.
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; 2.
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; 2.
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; Reference proteome; Transferase.
FT CHAIN 1..1055
FT /note="Cell-division control histidine kinase PdhS"
FT /id="PRO_0000361906"
FT DOMAIN 679..750
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 822..1051
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..626
FT /note="Important for polar localization"
FT /evidence="ECO:0000250"
FT REGION 419..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..1055
FT /note="Interaction with DivK"
FT /evidence="ECO:0000250"
FT MOD_RES 825
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 1055 AA; 113801 MW; B26569518A38029D CRC64;
MSGSYPFIDI AALDSIREGF AKGDAQLVLT HDLSAVLWVN GPGAKLFGFD RVEDMIGGGL
DLPIATRRQI ASSNSNAEGE TRTVSVRLGG GLRSDLTRFS VSHITLPDGV SGLLLTADGK
DAEAEDIISG LSDDSTHIAL IDANSRVIAA SPRFAALDIS STTLEDLVIE AADATDRIVK
RRIRAGKHSV PGAIARLTDT PPMHLLCIIG DAPVATLEAP AALQGEAEEI LEEILPEPVE
SANTEDASTD QQKPRSFVFE QDAPPARFIW KVGPDGTFSE ISPDLAATIG PNAADVVGRR
FADVANVFGF DPDGSIAALL DKRDTWSGKR LMWPVEGTDL RVPVELAALP VYSRDREFTG
FRGFGLVRPA EAEKDPEEIG LVLAGGIPQA RKPVSEPVET ATPVEDDDVL ALGEEVANDD
SPVATLPKPP LDIAPTPGRR ESDKVISLLN ACAEEKVAAD QARMLKERER EERPEGGLTK
TERNAFREIA DRLRKQGLAN SRAETETVAI SDEPVIDSSQ PVEKTEVKAS LIDEVTADEA
SLPSSGMAYG DETALLANLP VPVIIHSGDK IHYVNQALLD LTGYESLDDI RGAGGVDVLF
NSESDDGETR QGMVLRRANG SEEPVDAHLN AISWREGRAL MLSLMPVAAA PVSVEAVAAP
AEAPVAIDKD DEKQALADHV EELKTILDTA TDGVVLIDPE GRIRSMNHSA SALFGYERDE
TEGKFFSMLF AIESQRAAMD YLHGLSGNGV LSVLNDGREV IGREAKGGFI PLFMTIGKLP
HTRGFCAVLR DITQWKRTEE ELTNARKEAE RASSQKTEFL ARISHEIRTP LNAIIGFSEL
MADEKFGSIG NDRYRDYLRD INRSGNHVLA LVNDLLDISK IEAGALDMQF EAVSLNDAIA
EAIALMQPQA NRERVIIRSS FQSNLPDIVA DTRSIKQVAL NLLSNAVRFT APGGQVIVST
SYEMNGDVVM RVRDTGIGMT KSEVEQALKP FRQVNALERR KAETAKDWRS EGTGLGLPLT
KAMVEANRAQ FAIDSTPGHG TVVEIAFPPT RVLAD
