SSPC_STAA8
ID SSPC_STAA8 Reviewed; 109 AA.
AC Q9EYW6; Q2FZL4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Staphostatin B;
DE AltName: Full=Staphylococcal cysteine protease B inhibitor;
GN Name=sspC; OrderedLocusNames=SAOUHSC_00986;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11119502; DOI=10.1128/iai.69.1.159-169.2001;
RA Rice K., Peralta R., Bast D., de Azavedo J., McGavin M.J.;
RT "Description of Staphylococcus serine protease (ssp) operon in
RT Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine
RT protease.";
RL Infect. Immun. 69:159-169(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP PROTEIN SEQUENCE OF 1-8, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH STAPHOPAIN B.
RX PubMed=12890028; DOI=10.1046/j.1365-2958.2003.03613.x;
RA Rzychon M., Sabat A., Kosowska K., Potempa J., Dubin A.;
RT "Staphostatins: an expanding new group of proteinase inhibitors with a
RT unique specificity for the regulation of staphopains, Staphylococcus spp.
RT cysteine proteinases.";
RL Mol. Microbiol. 49:1051-1066(2003).
RN [4]
RP REGULATION.
RX PubMed=10517329; DOI=10.1007/s004380051090;
RA Lindsay J.A., Foster S.J.;
RT "Interactive regulatory pathways control virulence determinant production
RT and stability in response to environmental conditions in Staphylococcus
RT aureus.";
RL Mol. Gen. Genet. 262:323-331(1999).
RN [5]
RP INHIBITION BY SSPA.
RX PubMed=12207024; DOI=10.1074/jbc.m207162200;
RA Massimi I., Park E., Rice K., Mueller-Esterl W., Sauder D., McGavin M.J.;
RT "Identification of a novel maturation mechanism and restricted substrate
RT specificity for the sspB cysteine protease of Staphylococcus aureus.";
RL J. Biol. Chem. 277:41770-41777(2002).
RN [6]
RP INDUCTION.
RX PubMed=14702415; DOI=10.1099/mic.0.26634-0;
RA Shaw L., Golonka E., Potempa J., Foster S.J.;
RT "The role and regulation of the extracellular proteases of Staphylococcus
RT aureus.";
RL Microbiology 150:217-228(2004).
RN [7]
RP FUNCTION.
RX PubMed=15716447; DOI=10.1128/jb.187.5.1751-1762.2005;
RA Shaw L.N., Golonka E., Szmyd G., Foster S.J., Travis J., Potempa J.;
RT "Cytoplasmic control of premature activation of a secreted protease
RT zymogen: deletion of staphostatin B (sspC) in Staphylococcus aureus 8325-4
RT yields a profound pleiotropic phenotype.";
RL J. Bacteriol. 187:1751-1762(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH STAPHOPAIN B, AND
RP MUTAGENESIS OF GLY-98.
RX PubMed=12874290; DOI=10.1074/jbc.m302926200;
RA Filipek R., Rzychon M., Oleksy A., Gruca M., Dubin A., Potempa J.,
RA Bochtler M.;
RT "The staphostatin-staphopain complex: a forward binding inhibitor in
RT complex with its target cysteine protease.";
RL J. Biol. Chem. 278:40959-40966(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH STAPHOPAIN B.
RX PubMed=15644332; DOI=10.1074/jbc.m411792200;
RA Filipek R., Potempa J., Bochtler M.;
RT "A comparison of staphostatin B with standard mechanism serine protease
RT inhibitors.";
RL J. Biol. Chem. 280:14669-14674(2005).
CC -!- FUNCTION: Specifically inhibits the cysteine protease staphopain B
CC (SspB) by blocking the active site of the enzyme. Probably required to
CC protect cytoplasmic proteins from being degraded by prematurely
CC activated/folded prostaphopain B. Also involved in growth capacity,
CC viability and bacterial morphology. {ECO:0000269|PubMed:12890028,
CC ECO:0000269|PubMed:15716447}.
CC -!- SUBUNIT: Forms a stable non-covalent complex with prematurely
CC activated/folded SspB. {ECO:0000269|PubMed:12874290,
CC ECO:0000269|PubMed:15644332}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12890028}.
CC -!- INDUCTION: Expression occurs in a growth-phase-dependent manner with
CC optimal expression at post-exponential phase. Up-regulated by Agr
CC (accessory gene regulator) and repressed by SarA (staphylococcal
CC accessory regulator) and sigmaB factor. {ECO:0000269|PubMed:14702415}.
CC -!- MISCELLANEOUS: Inactivated by staphylococcal serine protease (SspA).
CC -!- MISCELLANEOUS: Disruption of sspC causes a total loss of secreted
CC extracellular proteins and a partial loss of peptidoglycan-associated
CC proteins. Loss of SspC results in profoundly reduced susceptibility of
CC peptidoglycan to lysis by lysostaphin.
CC -!- SIMILARITY: Belongs to the protease inhibitor I57 (SspC) family.
CC {ECO:0000305}.
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DR EMBL; AF309515; AAG45845.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30111.1; -; Genomic_DNA.
DR RefSeq; WP_000284457.1; NZ_LS483365.1.
DR RefSeq; YP_499539.1; NC_007795.1.
DR PDB; 1PXV; X-ray; 1.80 A; C/D=1-109.
DR PDB; 1Y4H; X-ray; 1.93 A; C/D=1-109.
DR PDBsum; 1PXV; -.
DR PDBsum; 1Y4H; -.
DR AlphaFoldDB; Q9EYW6; -.
DR SMR; Q9EYW6; -.
DR STRING; 1280.SAXN108_1044; -.
DR MEROPS; I57.001; -.
DR EnsemblBacteria; ABD30111; ABD30111; SAOUHSC_00986.
DR GeneID; 3920387; -.
DR KEGG; sao:SAOUHSC_00986; -.
DR PATRIC; fig|93061.5.peg.906; -.
DR eggNOG; ENOG50307R1; Bacteria.
DR HOGENOM; CLU_174854_0_0_9; -.
DR OMA; NTSHNQY; -.
DR EvolutionaryTrace; Q9EYW6; -.
DR PRO; PR:Q9EYW6; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.310.10; -; 1.
DR InterPro; IPR016085; Protease_inh_b-brl_dom.
DR InterPro; IPR037296; Staphostatin_A/B.
DR InterPro; IPR015113; Staphostatin_B.
DR Pfam; PF09023; Staphostatin_B; 1.
DR SUPFAM; SSF50882; SSF50882; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Protease inhibitor;
KW Reference proteome; Thiol protease inhibitor; Virulence.
FT CHAIN 1..109
FT /note="Staphostatin B"
FT /id="PRO_0000220553"
FT REGION 97..101
FT /note="Binds to staphopain B"
FT MUTAGEN 98
FT /note="G->A,R: Loss of affinity for SspB."
FT /evidence="ECO:0000269|PubMed:12874290"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1PXV"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1PXV"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:1PXV"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1PXV"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1PXV"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1PXV"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1PXV"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1PXV"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1PXV"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:1PXV"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:1PXV"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1PXV"
SQ SEQUENCE 109 AA; 12882 MW; A4D002333A614362 CRC64;
MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH NQYHILFIDT
AHQRIKFSSI DNEEIIYILD YDDTQHILMQ TSSKQGIGTS RPIVYERLV
