PHOR_BACSU
ID PHOR_BACSU Reviewed; 579 AA.
AC P23545;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Alkaline phosphatase synthesis sensor protein PhoR;
DE EC=2.7.13.3;
GN Name=phoR; OrderedLocusNames=BSU29100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3142862; DOI=10.1128/jb.170.12.5935-5938.1988;
RA Seki T., Yoshikawa H., Takahashi H., Saito H.;
RT "Nucleotide sequence of the Bacillus subtilis phoR gene.";
RL J. Bacteriol. 170:5935-5938(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SUBUNIT, INTERACTION WITH FLOA, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=25909364; DOI=10.1371/journal.pgen.1005140;
RA Schneider J., Klein T., Mielich-Suess B., Koch G., Franke C., Kuipers O.P.,
RA Kovacs A.T., Sauer M., Lopez D.;
RT "Spatio-temporal remodeling of functional membrane microdomains organizes
RT the signaling networks of a bacterium.";
RL PLoS Genet. 11:e1005140-e1005140(2015).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
CC -!- FUNCTION: Member of the two-component regulatory system PhoP/PhoR
CC involved in the alkaline phosphatase genes regulation. PhoR may
CC function as a membrane-associated protein kinase that phosphorylates
CC PhoP in 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 -!- SUBUNIT: Oligomerizes, probably forms homodimers. Interacts with FloA,
CC colocalizes with FloA-only membrane rafts. Oligomerization is assisted
CC by FloA (PubMed:25909364). Another study shows only minor
CC colocalization with FloA or FloT (PubMed:27362352).
CC {ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25909364,
CC ECO:0000305|PubMed:27362352}; Multi-pass membrane protein
CC {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:25909364,
CC ECO:0000305|PubMed:27362352}; Multi-pass membrane protein
CC {ECO:0000255}.
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DR EMBL; M23549; AAA22663.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00349.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14870.1; -; Genomic_DNA.
DR PIR; A27650; A27650.
DR RefSeq; NP_390788.1; NC_000964.3.
DR RefSeq; WP_004398493.1; NZ_JNCM01000036.1.
DR PDB; 3CWF; X-ray; 2.20 A; A/B=32-150.
DR PDBsum; 3CWF; -.
DR AlphaFoldDB; P23545; -.
DR SMR; P23545; -.
DR STRING; 224308.BSU29100; -.
DR PaxDb; P23545; -.
DR PRIDE; P23545; -.
DR DNASU; 937387; -.
DR EnsemblBacteria; CAB14870; CAB14870; BSU_29100.
DR GeneID; 937387; -.
DR KEGG; bsu:BSU29100; -.
DR PATRIC; fig|224308.179.peg.3159; -.
DR eggNOG; COG5002; Bacteria.
DR InParanoid; P23545; -.
DR OMA; MTETKKC; -.
DR PhylomeDB; P23545; -.
DR BioCyc; BSUB:BSU29100-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR EvolutionaryTrace; P23545; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
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; IPR031967; PhoR_single_Cache-like_dom.
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; PF16736; sCache_like; 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; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphate transport; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Transport; Two-component regulatory system.
FT CHAIN 1..579
FT /note="Alkaline phosphatase synthesis sensor protein PhoR"
FT /id="PRO_0000074845"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 234..300
FT /note="PAS"
FT DOMAIN 357..575
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 360
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT HELIX 35..53
FT /evidence="ECO:0007829|PDB:3CWF"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3CWF"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:3CWF"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3CWF"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3CWF"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3CWF"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:3CWF"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:3CWF"
SQ SEQUENCE 579 AA; 65122 MW; 0C4EE530A79A477B CRC64;
MNKYRVRLFS VFVVCMILVF CVLGLFLQQL FETSDQRKAE EHIEKEAKYL ASLLDAGNLN
NQANEKIIKD AGGALDVSAS VIDTDGKVLY GSNGRSADSQ KVQALVSGHE GILSTTDNKL
YYGLSLRSEG EKTGYVLLSA SEKSDGLKGE LWGMLTASLC TAFIVIVYFY SSMTSRYKRS
IESATNVATE LSKGNYDART YGGYIRRSDK LGHAMNSLAI DLMEMTRTQE MQRDRLLTVI
ENIGSGLIMI DGRGFINLVN RSYAKQFHIN PNHMLRRLYH DAFEHEEVIQ LVEDIFMTET
KKCKLLRLPI KIERRYFEVD GVPIMGPDDE WKGIVLVFHD MTETKKLEQM RKDFVANVSH
ELKTPITSIK GFTETLLDGA MEDKEALSEF LSIILKESER LQSLVQDLLD LSKIEQQNFT
LSIETFEPAK MLGEIETLLK HKADEKGISL HLNVPKDPQY VSGDPYRLKQ VFLNLVNNAL
TYTPEGGSVA INVKPREKDI QIEVADSGIG IQKEEIPRIF ERFYRVDKDR SRNSGGTGLG
LAIVKHLIEA HEGKIDVTSE LGRGTVFTVT LKRAAEKSA
