ID   SPXH_STAA8              Reviewed;         268 AA.
AC   Q2G203;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ClpXP adapter protein SpxH {ECO:0000255|HAMAP-Rule:MF_02245, ECO:0000305};
GN   Name=spxH {ECO:0000255|HAMAP-Rule:MF_02245};
GN   Synonyms=yjbH {ECO:0000303|PubMed:21947404};
GN   OrderedLocusNames=SAOUHSC_00938;
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 [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   [2]
RP   MUTANT STUDIES.
RX   PubMed=16923874; DOI=10.1128/jb.00551-06;
RA   Shaw L.N., Aish J., Davenport J.E., Brown M.C., Lithgow J.K., Simmonite K.,
RA   Crossley H., Travis J., Potempa J., Foster S.J.;
RT   "Investigations into sigmaB-modulated regulatory pathways governing
RT   extracellular virulence determinant production in Staphylococcus aureus.";
RL   J. Bacteriol. 188:6070-6080(2006).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-121 AND CYS-123.
RC   STRAIN=ATCC 35556 / SA113;
RX   PubMed=21947404; DOI=10.1128/aac.00286-11;
RA   Goehring N., Fedtke I., Xia G., Jorge A.M., Pinho M.G., Bertsche U.,
RA   Peschel A.;
RT   "New role of the disulfide stress effector YjbH in beta-lactam
RT   susceptibility of Staphylococcus aureus.";
RL   Antimicrob. Agents Chemother. 55:5452-5458(2011).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NCTC 8325-4;
RX   PubMed=22194450; DOI=10.1128/jb.06414-11;
RA   Engman J., Rogstam A., Frees D., Ingmer H., von Wachenfeldt C.;
RT   "The YjbH adaptor protein enhances proteolysis of the transcriptional
RT   regulator Spx in Staphylococcus aureus.";
RL   J. Bacteriol. 194:1186-1194(2012).
RN   [5]
RP   FUNCTION, AND ACTIVITY REGULATION.
RC   STRAIN=HG003;
RX   PubMed=32117138; DOI=10.3389/fmicb.2020.00113;
RA   Panasenko O.O., Bezrukov F., Komarynets O., Renzoni A.;
RT   "YjbH solubility controls Spx in Staphylococcus aureus: implication for
RT   MazEF toxin-antitoxin system regulation.";
RL   Front. Microbiol. 11:113-113(2020).
CC   -!- FUNCTION: Adapter protein required for efficient degradation of Spx by
CC       ClpXP under non-stress conditions (PubMed:22194450, PubMed:32117138).
CC       Interaction with Spx stabilizes Spx and exposes the C-terminus of Spx
CC       for recognition and proteolysis by ClpXP (By similarity). Involved in
CC       disulfide stress regulation (PubMed:21947404).
CC       {ECO:0000250|UniProtKB:O31606, ECO:0000269|PubMed:21947404,
CC       ECO:0000269|PubMed:22194450, ECO:0000269|PubMed:32117138}.
CC   -!- ACTIVITY REGULATION: In non-stressed conditions, mainly remains soluble
CC       (PubMed:32117138). Forms aggregates in response to different
CC       environmental stresses such as heat shock, oxidative stress and
CC       antibiotic treatment, and cannot assist Spx degradation
CC       (PubMed:32117138). {ECO:0000269|PubMed:32117138}.
CC   -!- SUBUNIT: Interacts with Spx. {ECO:0000255|HAMAP-Rule:MF_02245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02245}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the gene increases the level of
CC       Spx protein and transcription of the Spx-regulated gene trxB
CC       (PubMed:22194450). Disruption leads to an increase in hla (alpha-
CC       hemolysin) transcription and proteases production (PubMed:16923874). It
CC       also leads to increased tolerance to the disulfide stress inducing
CC       compound diamide, increased peptidoglycan cross-linking, and moderate
CC       resistance to oxacillin and other beta-lactams antibiotics
CC       (PubMed:21947404). {ECO:0000269|PubMed:16923874,
CC       ECO:0000269|PubMed:21947404, ECO:0000269|PubMed:22194450}.
CC   -!- MISCELLANEOUS: Goehring et al. suggest that the cysteine residues are
CC       important for the role of YjbH/SpxH in disulfide stress management
CC       (PubMed:21947404). However, mutation of all seven cysteine residues in
CC       B.subtilis ortholog by Engman et al. shows that these cysteines are
CC       dispensable for the function of the protein and that the activity of
CC       the adapter is not activated or deactivated via redox-active cysteines
CC       (PubMed:22194450). {ECO:0000269|PubMed:21947404,
CC       ECO:0000269|PubMed:22194450}.
CC   -!- SIMILARITY: Belongs to the SpxH family. {ECO:0000255|HAMAP-
CC       Rule:MF_02245}.
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DR   EMBL; CP000253; ABD30063.1; -; Genomic_DNA.
DR   RefSeq; WP_000896697.1; NZ_LS483365.1.
DR   RefSeq; YP_499491.1; NC_007795.1.
DR   AlphaFoldDB; Q2G203; -.
DR   SMR; Q2G203; -.
DR   STRING; 1280.SAXN108_0998; -.
DR   EnsemblBacteria; ABD30063; ABD30063; SAOUHSC_00938.
DR   GeneID; 3920767; -.
DR   KEGG; sao:SAOUHSC_00938; -.
DR   PATRIC; fig|93061.5.peg.859; -.
DR   eggNOG; COG2761; Bacteria.
DR   HOGENOM; CLU_069785_0_0_9; -.
DR   OMA; YRMGGLL; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   HAMAP; MF_02245; Adapter_SpxH; 1.
DR   InterPro; IPR046404; Adapter_SpxH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..268
FT                   /note="ClpXP adapter protein SpxH"
FT                   /id="PRO_0000278689"
FT   MUTAGEN         121
FT                   /note="C->G: Cannot restore wild-type level diamide
FT                   susceptibility to the deletion mutant."
FT                   /evidence="ECO:0000269|PubMed:21947404"
FT   MUTAGEN         123
FT                   /note="C->G: Cannot restore wild-type level diamide
FT                   susceptibility to the deletion mutant."
FT                   /evidence="ECO:0000269|PubMed:21947404"
SQ   SEQUENCE   268 AA;  31364 MW;  F40B877860BD1140 CRC64;
     MAGELRIMEN KSREDINLSP VSKIEIYSFF DPFSSDCFKL SAILSKLRIE YNQYIRIRHI
     LNPSLKVLTK CQAQSTSNFD NIALAYKAAE LQGRVRAERF IHLMQNEIIP KRDIITESMI
     CDCIQNAGID LEVFKDDLQK SKLTESLKID LHIAREMEIE QAPSLVFFSE DVHEEGLKVE
     GLYPYHIYTY IINELMGKPI EKNLPPKLET YIQQQQLVTM EELLTIYEWP EKLLNKELKK
     LAIQQKIEKL KYPDGDFWKS KMPKIKSK