ID   A4G9H1_HERAR            Unreviewed;       203 AA.
AC   A4G9H1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Stringent starvation protein A {ECO:0000313|EMBL:CAL63158.1};
GN   OrderedLocusNames=HEAR3049 {ECO:0000313|EMBL:CAL63158.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL63158.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL63158.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
CC   -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC       {ECO:0000256|ARBA:ARBA00009929}.
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DR   EMBL; CU207211; CAL63158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G9H1; -.
DR   STRING; 204773.HEAR3049; -.
DR   KEGG; har:HEAR3049; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_9_3_4; -.
DR   OrthoDB; 9781431at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   CDD; cd03059; GST_N_SspA; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR034341; SspA_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43968; -; 1.
DR   PANTHER; PTHR43968:SF6; GLUTATHIONE S-TRANSFERASE OMEGA; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006697}.
FT   DOMAIN          1..78
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          83..203
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   203 AA;  23778 MW;  BA27BE116C4530C8 CRC64;
     MMVLYSGTTC PFSQRCRLVL FEKGMDFEVR DVDLFNKPED ISTMNPYGQV PILVERDLIL
     YESNIINEYI DERFPHPQLM PADPLMRARA RLMLFNFEKE LFIHVHVLEN DKGRSGEKAQ
     EKARNEIRDR LTTLAPLFLK NKYMLGDEFS MLDVAIAPLL WRLDHYGIEL SKTAAPLMKY
     AERIFSRPAY IEALTPSEKV MRR
//