PDHS_BRUME
ID PDHS_BRUME Reviewed; 1035 AA.
AC Q8YIM6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cell-division control histidine kinase PdhS;
DE EC=2.7.13.3;
GN Name=pdhS; OrderedLocusNames=BMEI0417;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL51598.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL51598.1; ALT_INIT; Genomic_DNA.
DR PIR; AC3304; AC3304.
DR RefSeq; WP_004684102.1; NZ_GG703780.1.
DR AlphaFoldDB; Q8YIM6; -.
DR SMR; Q8YIM6; -.
DR STRING; 224914.BMEI0417; -.
DR EnsemblBacteria; AAL51598; AAL51598; BMEI0417.
DR GeneID; 29593193; -.
DR KEGG; bme:BMEI0417; -.
DR PATRIC; fig|224914.52.peg.1063; -.
DR eggNOG; COG2205; Bacteria.
DR PhylomeDB; Q8YIM6; -.
DR Proteomes; UP000000419; 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_0000361902"
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; 111799 MW; CB622B372DC034CA 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 VFGFDTDGSI AALLLERDTW SGKRLLWPVE GTRLRVPVEL AALPVYSRDR
EFLGFRGFGI VRPAEAEADP EEIGLALAGG IPQNRKPRKE PAETARMVGE DDVLALSEEV
ANDDHPAAVL PKPPLDITPT PGRRDSDKVI SLLNSCAQEK VAANQAKFLK 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 FRQINALERR KAESAKDWRN EGTGLGLPLT KAMVEANRAQ FAIDSNPGQG
TVVEIVFPPT RVLAD
