ID   SSPA_ECOLI              Reviewed;         212 AA.
AC   P0ACA3; P05838; Q2M8Y4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Stringent starvation protein A;
GN   Name=sspA; Synonyms=pog, ssp; OrderedLocusNames=b3229, JW3198;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3029697; DOI=10.1093/nar/15.3.1153;
RA   Serizawa H., Fukuda R.;
RT   "Structure of the gene for the stringent starvation protein of Escherichia
RT   coli.";
RL   Nucleic Acids Res. 15:1153-1163(1987).
RN   [2]
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   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=8022275; DOI=10.1111/j.1365-2958.1994.tb00381.x;
RA   Williams M.D., Ouyang T.X., Flickinger M.C.;
RT   "Starvation-induced expression of SspA and SspB: the effects of a null
RT   mutation in sspA on Escherichia coli protein synthesis and survival during
RT   growth and prolonged starvation.";
RL   Mol. Microbiol. 11:1029-1043(1994).
RN   [6]
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).
CC   -!- FUNCTION: Forms an equimolar complex with the RNA polymerase holoenzyme
CC       (RNAP) but not with the core enzyme. It is synthesized predominantly
CC       when cells are exposed to amino acid starvation, at which time it
CC       accounts for over 50% of the total protein synthesized. It is involved
CC       in the transition from P1 early to P1 late gene expression. Rnk and
CC       SspA can functionally replace P.aeruginosa alginate regulatory gene
CC       algR2.
CC   -!- INTERACTION:
CC       P0ACA3; P54745: mngA; NbExp=5; IntAct=EBI-558482, EBI-558542;
CC   -!- INDUCTION: By amino acid starvation.
CC   -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X05088; CAA28740.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58031.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76261.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77272.1; -; Genomic_DNA.
DR   PIR; A26422; RGECSS.
DR   RefSeq; NP_417696.1; NC_000913.3.
DR   RefSeq; WP_000257293.1; NZ_STEB01000012.1.
DR   PDB; 6WMU; EM; 3.18 A; K/L=1-212.
DR   PDB; 7C97; EM; 3.68 A; I/J=1-212.
DR   PDB; 7DY6; EM; 3.68 A; I/J=1-212.
DR   PDBsum; 6WMU; -.
DR   PDBsum; 7C97; -.
DR   PDBsum; 7DY6; -.
DR   AlphaFoldDB; P0ACA3; -.
DR   SMR; P0ACA3; -.
DR   BioGRID; 4262445; 18.
DR   BioGRID; 849148; 2.
DR   DIP; DIP-48104N; -.
DR   IntAct; P0ACA3; 13.
DR   STRING; 511145.b3229; -.
DR   TCDB; 1.A.12.3.1; the intracellular chloride channel (clic) family.
DR   SWISS-2DPAGE; P0ACA3; -.
DR   jPOST; P0ACA3; -.
DR   PaxDb; P0ACA3; -.
DR   PRIDE; P0ACA3; -.
DR   EnsemblBacteria; AAC76261; AAC76261; b3229.
DR   EnsemblBacteria; BAE77272; BAE77272; BAE77272.
DR   GeneID; 67415939; -.
DR   GeneID; 944744; -.
DR   KEGG; ecj:JW3198; -.
DR   KEGG; eco:b3229; -.
DR   PATRIC; fig|1411691.4.peg.3499; -.
DR   EchoBASE; EB0970; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_9_3_6; -.
DR   InParanoid; P0ACA3; -.
DR   OMA; ADHYSHR; -.
DR   PhylomeDB; P0ACA3; -.
DR   BioCyc; EcoCyc:EG10977-MON; -.
DR   PRO; PR:P0ACA3; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
DR   GO; GO:0042594; P:response to starvation; IEP:EcoCyc.
DR   CDD; cd03186; GST_C_SspA; 1.
DR   CDD; cd03059; GST_N_SspA; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR034342; SspA_C.
DR   InterPro; IPR034341; SspA_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298646"
FT   CHAIN           2..212
FT                   /note="Stringent starvation protein A"
FT                   /id="PRO_0000185876"
FT   DOMAIN          9..87
FT                   /note="GST N-terminal"
FT   DOMAIN          92..209
FT                   /note="GST C-terminal"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           20..32
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           48..53
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           72..82
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           93..119
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           122..143
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           156..166
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   TURN            167..172
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           178..192
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           194..199
FT                   /evidence="ECO:0007829|PDB:6WMU"
FT   HELIX           202..205
FT                   /evidence="ECO:0007829|PDB:6WMU"
SQ   SEQUENCE   212 AA;  24305 MW;  A0FFA98F7131B34F CRC64;
     MAVAANKRSV MTLFSGPTDI YSHQVRIVLA EKGVSFEIEH VEKDNPPQDL IDLNPNQSVP
     TLVDRELTLW ESRIIMEYLD ERFPHPPLMP VYPVARGESR LYMHRIEKDW YTLMNTIING
     SASEADAARK QLREELLAIA PVFGQKPYFL SDEFSLVDCY LAPLLWRLPQ LGIEFSGPGA
     KELKGYMTRV FERDSFLASL TEAEREMRLG RS