PSPF_ECOLI
ID PSPF_ECOLI Reviewed; 325 AA.
AC P37344; P76039;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Psp operon transcriptional activator;
DE AltName: Full=Phage shock protein F;
GN Name=pspF; Synonyms=ycjB; OrderedLocusNames=b1303, JW1296;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=8606168; DOI=10.1128/jb.178.7.1936-1945.1996;
RA Jovanovic G., Weiner L., Model P.;
RT "Identification, nucleotide sequence, and characterization of PspF, the
RT transcriptional activator of the Escherichia coli stress-induced psp
RT operon.";
RL J. Bacteriol. 178:1936-1945(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-110.
RC STRAIN=K12;
RX PubMed=1712397; DOI=10.1016/0022-2836(91)90379-k;
RA Brissette J.L., Weiner L., Ripmaster T.L., Model P.;
RT "Characterization and sequence of the Escherichia coli stress-induced psp
RT operon.";
RL J. Mol. Biol. 220:35-48(1991).
RN [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
RP IDENTIFICATION.
RX PubMed=7920643; DOI=10.1038/ng0694-205;
RA Robison K., Gilbert W., Church G.M.;
RT "Large scale bacterial gene discovery by similarity search.";
RL Nat. Genet. 7:205-214(1994).
RN [8]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15485810; DOI=10.1074/jbc.m408994200;
RA Lloyd L.J., Jones S.E., Jovanovic G., Gyaneshwar P., Rolfe M.D.,
RA Thompson A., Hinton J.C., Buck M.;
RT "Identification of a new member of the phage shock protein response in
RT Escherichia coli, the phage shock protein G (PspG).";
RL J. Biol. Chem. 279:55707-55714(2004).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH PSPA.
RX PubMed=19804784; DOI=10.1016/j.jmb.2009.09.055;
RA Joly N., Burrows P.C., Engl C., Jovanovic G., Buck M.;
RT "A lower-order oligomer form of phage shock protein A (PspA) stably
RT associates with the hexameric AAA(+) transcription activator protein PspF
RT for negative regulation.";
RL J. Mol. Biol. 394:764-775(2009).
CC -!- FUNCTION: Transcriptional activator for the phage shock protein (psp)
CC operon (pspABCDE) and pspG gene. {ECO:0000269|PubMed:15485810,
CC ECO:0000269|PubMed:19804784, ECO:0000269|PubMed:8606168}.
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by interaction with
CC PspA. Under inducing conditions, the interaction is disrupted, allowing
CC activation of psp transcription. {ECO:0000269|PubMed:19804784}.
CC -!- SUBUNIT: Forms a complex with PspA, which is composed of around 6 PspF
CC subunits and 6 PspA subunits. {ECO:0000269|PubMed:19804784}.
CC -!- INTERACTION:
CC P37344; P0AFM6: pspA; NbExp=6; IntAct=EBI-1123431, EBI-1123459;
CC P37344; P37344: pspF; NbExp=2; IntAct=EBI-1123431, EBI-1123431;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; U38542; AAB02186.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74385.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14872.1; -; Genomic_DNA.
DR EMBL; X57560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B64879; B64879.
DR RefSeq; NP_415819.4; NC_000913.3.
DR RefSeq; WP_001301108.1; NZ_SSZK01000012.1.
DR PDB; 2BJV; X-ray; 1.70 A; A=1-265.
DR PDB; 2BJW; X-ray; 1.75 A; A=1-265.
DR PDB; 2C96; X-ray; 1.80 A; A=1-265.
DR PDB; 2C98; X-ray; 1.90 A; A=1-265.
DR PDB; 2C99; X-ray; 1.90 A; A=1-265.
DR PDB; 2C9C; X-ray; 2.10 A; A=1-265.
DR PDB; 2VII; X-ray; 2.85 A; A=1-259.
DR PDB; 4QNM; X-ray; 1.63 A; A=1-265.
DR PDB; 4QNR; X-ray; 1.54 A; A=1-265.
DR PDB; 4QOS; X-ray; 1.42 A; A=1-265.
DR PDB; 5NSS; EM; 5.80 A; F/G/J/K/L/N=1-275.
DR PDBsum; 2BJV; -.
DR PDBsum; 2BJW; -.
DR PDBsum; 2C96; -.
DR PDBsum; 2C98; -.
DR PDBsum; 2C99; -.
DR PDBsum; 2C9C; -.
DR PDBsum; 2VII; -.
DR PDBsum; 4QNM; -.
DR PDBsum; 4QNR; -.
DR PDBsum; 4QOS; -.
DR PDBsum; 5NSS; -.
DR AlphaFoldDB; P37344; -.
DR SMR; P37344; -.
DR BioGRID; 4263525; 650.
DR ComplexPortal; CPX-5745; pspAF transcription regulation complex.
DR DIP; DIP-10592N; -.
DR IntAct; P37344; 4.
DR STRING; 511145.b1303; -.
DR jPOST; P37344; -.
DR PaxDb; P37344; -.
DR PRIDE; P37344; -.
DR EnsemblBacteria; AAC74385; AAC74385; b1303.
DR EnsemblBacteria; BAA14872; BAA14872; BAA14872.
DR GeneID; 945683; -.
DR KEGG; ecj:JW1296; -.
DR KEGG; eco:b1303; -.
DR PATRIC; fig|1411691.4.peg.976; -.
DR EchoBASE; EB2248; -.
DR eggNOG; COG1221; Bacteria.
DR HOGENOM; CLU_000445_0_7_6; -.
DR InParanoid; P37344; -.
DR OMA; YHQFRGL; -.
DR PhylomeDB; P37344; -.
DR BioCyc; EcoCyc:EG12344-MON; -.
DR EvolutionaryTrace; P37344; -.
DR PRO; PR:P37344; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0080135; P:regulation of cellular response to stress; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR InterPro; IPR014317; Transcription_activator_PspF.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02974; phageshock_pspF; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; Cytoplasm; DNA-binding;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..325
FT /note="Psp operon transcriptional activator"
FT /id="PRO_0000081329"
FT DOMAIN 15..237
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 302..321
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 99..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:4QOS"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:4QOS"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:4QOS"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4QOS"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:4QNR"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:4QOS"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4QOS"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:4QOS"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2C96"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4QNM"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:4QOS"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4QOS"
FT HELIX 225..240
FT /evidence="ECO:0007829|PDB:4QOS"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4QOS"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2C96"
SQ SEQUENCE 325 AA; 36986 MW; F495D634193A42FB CRC64;
MAEYKDNLLG EANSFLEVLE QVSHLAPLDK PVLIIGERGT GKELIASRLH YLSSRWQGPF
ISLNCAALNE NLLDSELFGH EAGAFTGAQK RHPGRFERAD GGTLFLDELA TAPMMVQEKL
LRVIEYGELE RVGGSQPLQV NVRLVCATNA DLPAMVNEGT FRADLLDRLA FDVVQLPPLR
ERESDIMLMA EYFAIQMCRE IKLPLFPGFT ERARETLLNY RWPGNIRELK NVVERSVYRH
GTSDYPLDDI IIDPFKRRPP EDAIAVSETT SLPTLPLDLR EFQMQQEKEL LQLSLQQGKY
NQKRAAELLG LTYHQFRALL KKHQI
