PHOR_PSEAE
ID PHOR_PSEAE Reviewed; 443 AA.
AC P23621;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Phosphate regulon sensor protein PhoR;
DE EC=2.7.13.3;
GN Name=phoR; OrderedLocusNames=PA5361;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
RX PubMed=2115874; DOI=10.1128/jb.172.8.4685-4689.1990;
RA Anba J., Bidaud M., Vasil M.L., Lazdunski A.;
RT "Nucleotide sequence of the Pseudomonas aeruginosa phoB gene, the
RT regulatory gene for the phosphate regulon.";
RL J. Bacteriol. 172:4685-4689(1990).
CC -!- FUNCTION: Member of the two-component regulatory system PhoR/PhoB
CC involved in the phosphate regulon genes expression. PhoR may function
CC as a membrane-associated protein kinase that phosphorylates PhoB in
CC response to environmental signals.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AE004091; AAG08746.1; -; Genomic_DNA.
DR PIR; B37775; B37775.
DR PIR; D82975; D82975.
DR RefSeq; NP_254048.1; NC_002516.2.
DR RefSeq; WP_003121316.1; NZ_QZGE01000020.1.
DR AlphaFoldDB; P23621; -.
DR SMR; P23621; -.
DR STRING; 287.DR97_2732; -.
DR PaxDb; P23621; -.
DR EnsemblBacteria; AAG08746; AAG08746; PA5361.
DR GeneID; 878511; -.
DR KEGG; pae:PA5361; -.
DR PATRIC; fig|208964.12.peg.5618; -.
DR PseudoCAP; PA5361; -.
DR HOGENOM; CLU_000445_89_2_6; -.
DR InParanoid; P23621; -.
DR OMA; TRFWRGS; -.
DR PhylomeDB; P23621; -.
DR BioCyc; PAER208964:G1FZ6-5483-MON; -.
DR BRENDA; 2.7.13.3; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; 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; IPR021766; PhoR.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR014310; Sig_transdc_His_kinase_PhoR.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF11808; PhoR; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR02966; phoR_proteo; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphate transport; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Transport;
KW Two-component regulatory system.
FT CHAIN 1..443
FT /note="Phosphate regulon sensor protein PhoR"
FT /id="PRO_0000074849"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 93..182
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 216..433
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 219
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 38
FT /note="L -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="A -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="R -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50120 MW; 4ABCDAE58D9733E2 CRC64;
MQSVVNQDWR GALIRHLLLV LAASLVLGVV SGHYGWALAL GLALYLGWTL WQLLRLHQWL
RNHQPDEPPP DSYGLWGEVF DNIYHLQRRN QRARGRLQAV IDRIQESTAA LRDAVIMLDS
DGNLEWWNLA AENLLGLKTP QDGGQPVSNL IRHPRFKEYF DQEDYREPLE IPSPINERLR
LQFHITLYGN REHLMLVRDV TRVHQLEQMR KDFVANVSHE LRTPLTVIAG YLETLLDNVE
DVNPRWLRAL QQMQQQAGRM QNLLNDLLLL AKLEATDYPG DNKPVAVDAL LASIRNDAQA
LSAGRNHRIS LDAAPAVQLK GSEAELRSAF SNLVFNAVKY TPDEGEIRIR WWADEQGAHL
SVQDTGIGVD PKHLPRLTER FYRVDSSRAS NTGGTGLGLA IVKHVLIRHR ARLEISSVPG
KGSTFTCHFA PAQVAEAERK APK
