ID A9HW87_BORPD Unreviewed; 203 AA.
AC A9HW87;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Stringent starvation protein A {ECO:0000313|EMBL:CAP40450.1};
GN Name=sspA {ECO:0000313|EMBL:CAP40450.1};
GN OrderedLocusNames=Bpet0119 {ECO:0000313|EMBL:CAP40450.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP40450.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP40450.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC {ECO:0000256|ARBA:ARBA00009929}.
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DR EMBL; AM902716; CAP40450.1; -; Genomic_DNA.
DR AlphaFoldDB; A9HW87; -.
DR STRING; 94624.Bpet0119; -.
DR KEGG; bpt:Bpet0119; -.
DR eggNOG; COG0625; Bacteria.
DR Proteomes; UP000001225; 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;
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; 23806 MW; 678C84F06E5C2158 CRC64;
MMVLYSGTTC PFSQRCRFVL FEKGMDFEIR DIDLYNKPED ISVMNPYGQV PILVERDLVL
YESNIINEYI DERFPHPQLM PADPVMRART RLFLYNFEKE LFVHVSTLED RSAKPDEKKL
ATARQNIRDR LAQLAPLLLK NKYMLGDEFS MLDVAVAPLL WRLDHYGIEL PKNAAPLQKY
AERIFSRPAY IEALTPSEKV MRR
//
