PSPA_ECOLI
ID PSPA_ECOLI Reviewed; 222 AA.
AC P0AFM6; P23853; P76040; P77363;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phage shock protein A;
GN Name=pspA; OrderedLocusNames=b1304, JW1297;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP INDUCTION.
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 [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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=7921245; DOI=10.1099/13500872-140-8-1937;
RA Bergler H., Abraham D., Aschauer H., Turnowsky F.;
RT "Inhibition of lipid biosynthesis induces the expression of the pspA
RT gene.";
RL Microbiology 140:1937-1944(1994).
RN [6]
RP PROTEIN SEQUENCE OF 2-20.
RC STRAIN=K12 / JA300 / ATCC 33588 / DSM 4776 / NCIMB 12220;
RX PubMed=9493373; DOI=10.1099/00221287-144-2-353;
RA Kobayashi H., Yamamoto M., Aono R.;
RT "Appearance of a stress-response protein, phage-shock protein A, in
RT Escherichia coli exposed to hydrophobic organic solvents.";
RL Microbiology 144:353-359(1998).
RN [7]
RP FUNCTION.
RX PubMed=8598199; DOI=10.1002/j.1460-2075.1996.tb00344.x;
RA Kleerebezem M., Crielaard W., Tommassen J.;
RT "Involvement of stress protein PspA (phage shock protein A) of Escherichia
RT coli in maintenance of the protonmotive force under stress conditions.";
RL EMBO J. 15:162-171(1996).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP FUNCTION.
RX PubMed=10629175; DOI=10.1128/jb.182.2.311-319.2000;
RA Dworkin J., Jovanovic G., Model P.;
RT "The PspA protein of Escherichia coli is a negative regulator of sigma(54)-
RT dependent transcription.";
RL J. Bacteriol. 182:311-319(2000).
RN [10]
RP INTERACTION WITH PSPB AND PSPC.
RC STRAIN=K12;
RX PubMed=12562786; DOI=10.1128/jb.185.4.1174-1180.2003;
RA Adams H., Teertstra W., Demmers J., Boesten R., Tommassen J.;
RT "Interactions between phage-shock proteins in Escherichia coli.";
RL J. Bacteriol. 185:1174-1180(2003).
RN [11]
RP SUBUNIT.
RX PubMed=14688274; DOI=10.1074/jbc.m307889200;
RA Hankamer B.D., Elderkin S.L., Buck M., Nield J.;
RT "Organization of the AAA(+) adaptor protein PspA is an oligomeric ring.";
RL J. Biol. Chem. 279:8862-8866(2004).
RN [12]
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 [13]
RP INDUCTION BY CDI, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=19124575; DOI=10.1128/jb.01437-08;
RA Aoki S.K., Webb J.S., Braaten B.A., Low D.A.;
RT "Contact-dependent growth inhibition causes reversible metabolic
RT downregulation in Escherichia coli.";
RL J. Bacteriol. 191:1777-1786(2009).
RN [14]
RP FUNCTION, SUBUNIT, INTERACTION WITH PSPF, AND DOMAIN.
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).
RN [15]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19555453; DOI=10.1111/j.1365-2958.2009.06776.x;
RA Engl C., Jovanovic G., Lloyd L.J., Murray H., Spitaler M., Ying L.,
RA Errington J., Buck M.;
RT "In vivo localizations of membrane stress controllers PspA and PspG in
RT Escherichia coli.";
RL Mol. Microbiol. 73:382-396(2009).
CC -!- FUNCTION: The phage shock protein (psp) operon (pspABCDE) may play a
CC significant role in the competition for survival under nutrient- or
CC energy-limited conditions. PspA negatively regulates expression of the
CC pspABCDE promoter and of pspG through negative regulation of the psp-
CC specific transcriptional activator PspF. Is also required for membrane
CC integrity, efficient translocation and maintenance of the proton motive
CC force. {ECO:0000269|PubMed:10629175, ECO:0000269|PubMed:15485810,
CC ECO:0000269|PubMed:1712397, ECO:0000269|PubMed:19804784,
CC ECO:0000269|PubMed:8598199}.
CC -!- SUBUNIT: Exists in at least two different oligomeric assemblies.
CC Regulatory function involves the formation of a complex with PspF,
CC which is composed of around 6 PspF subunits and 6 PspA subunits.
CC Maintenance of membrane integrity involves the formation of a 36-mer
CC ring complex. Interacts with PspB and PspC.
CC {ECO:0000269|PubMed:12562786, ECO:0000269|PubMed:14688274,
CC ECO:0000269|PubMed:19804784}.
CC -!- INTERACTION:
CC P0AFM6; P0AFM6: pspA; NbExp=5; IntAct=EBI-1123459, EBI-1123459;
CC P0AFM6; P0AFN2: pspC; NbExp=9; IntAct=EBI-1123459, EBI-1134561;
CC P0AFM6; P37344: pspF; NbExp=6; IntAct=EBI-1123459, EBI-1123431;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19555453}. Cell
CC inner membrane {ECO:0000269|PubMed:19555453}; Peripheral membrane
CC protein {ECO:0000269|PubMed:19555453}; Cytoplasmic side
CC {ECO:0000269|PubMed:19555453}. Note=Localizes at both cell poles and
CC along the length of the cell.
CC -!- INDUCTION: By heat, ethanol, osmotic shock and infection by filamentous
CC bacteriophages (PubMed:1712397). Induced during contact-dependent
CC growth inhibition (CDI), but not during recovery from CDI
CC (PubMed:19124575). {ECO:0000269|PubMed:1712397,
CC ECO:0000269|PubMed:19124575}.
CC -!- DOMAIN: All four putative helical domains of PspA are critical for the
CC formation of the 36-mer. In contrast, not all four helical domains are
CC required for the formation of the inhibitory PspA-PspF complex.
CC {ECO:0000269|PubMed:19804784}.
CC -!- DISRUPTION PHENOTYPE: Not required for induction of, or recovery from,
CC contact-dependent growth inhibition (CDI).
CC {ECO:0000269|PubMed:19124575}.
CC -!- SIMILARITY: Belongs to the PspA/IM30 family. {ECO:0000305}.
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DR EMBL; X57560; CAA40789.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74386.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14873.1; -; Genomic_DNA.
DR PIR; C64879; C64879.
DR RefSeq; NP_415820.1; NC_000913.3.
DR RefSeq; WP_000511025.1; NZ_SSZK01000012.1.
DR PDB; 4WHE; X-ray; 1.80 A; A=1-144.
DR PDBsum; 4WHE; -.
DR AlphaFoldDB; P0AFM6; -.
DR SMR; P0AFM6; -.
DR BioGRID; 4262874; 308.
DR ComplexPortal; CPX-5745; pspAF transcription regulation complex.
DR DIP; DIP-10587N; -.
DR IntAct; P0AFM6; 6.
DR STRING; 511145.b1304; -.
DR jPOST; P0AFM6; -.
DR PaxDb; P0AFM6; -.
DR PRIDE; P0AFM6; -.
DR EnsemblBacteria; AAC74386; AAC74386; b1304.
DR EnsemblBacteria; BAA14873; BAA14873; BAA14873.
DR GeneID; 66674868; -.
DR GeneID; 945887; -.
DR KEGG; ecj:JW1297; -.
DR KEGG; eco:b1304; -.
DR PATRIC; fig|1411691.4.peg.975; -.
DR EchoBASE; EB0769; -.
DR eggNOG; COG1842; Bacteria.
DR HOGENOM; CLU_056466_3_0_6; -.
DR InParanoid; P0AFM6; -.
DR OMA; MIFRAKA; -.
DR PhylomeDB; P0AFM6; -.
DR BioCyc; EcoCyc:EG10776-MON; -.
DR PRO; PR:P0AFM6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0060187; C:cell pole; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0005543; F:phospholipid binding; IDA:EcoCyc.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0009271; P:phage shock; IEP:EcoliWiki.
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 GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR InterPro; IPR014319; Phageshock_PspA.
DR InterPro; IPR007157; PspA_IM30.
DR PANTHER; PTHR31088; PTHR31088; 1.
DR Pfam; PF04012; PspA_IM30; 1.
DR TIGRFAMs; TIGR02977; phageshock_pspA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Membrane; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9493373"
FT CHAIN 2..222
FT /note="Phage shock protein A"
FT /id="PRO_0000166292"
FT COILED 30..187
FT /evidence="ECO:0000255"
FT COILED 204..222
FT /evidence="ECO:0000255"
FT CONFLICT 182
FT /note="A -> R (in Ref. 1; CAA40789)"
FT /evidence="ECO:0000305"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:4WHE"
FT HELIX 25..80
FT /evidence="ECO:0007829|PDB:4WHE"
FT HELIX 84..141
FT /evidence="ECO:0007829|PDB:4WHE"
SQ SEQUENCE 222 AA; 25493 MW; EAC29290406E5053 CRC64;
MGIFSRFADI VNANINALLE KAEDPQKLVR LMIQEMEDTL VEVRSTSARA LAEKKQLTRR
IEQASAREVE WQEKAELALL KEREDLARAA LIEKQKLTDL IKSLEHEVTL VDDTLARMKK
EIGELENKLS ETRARQQALM LRHQAANSSR DVRRQLDSGK LDEAMARFES FERRIDQMEA
EAESHSFGKQ KSLDDQFAEL KADDAISEQL AQLKAKMKQD NQ
