SPXH_BACSU
ID SPXH_BACSU Reviewed; 299 AA.
AC O31606;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ClpXP adapter protein SpxH {ECO:0000255|HAMAP-Rule:MF_02245, ECO:0000305};
GN Name=spxH {ECO:0000255|HAMAP-Rule:MF_02245, ECO:0000312|EMBL:CAB13012.2};
GN Synonyms=yjbH; OrderedLocusNames=BSU11550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17908206; DOI=10.1111/j.1365-2958.2007.05949.x;
RA Larsson J.T., Rogstam A., von Wachenfeldt C.;
RT "YjbH is a novel negative effector of the disulphide stress regulator, Spx,
RT in Bacillus subtilis.";
RL Mol. Microbiol. 66:669-684(2007).
RN [3]
RP FUNCTION, ZINC-BINDING, INTERACTION WITH SPX, DOMAIN, AND MUTAGENESIS OF
RP 1-MET--TYR-24.
RC STRAIN=168 / JH642;
RX PubMed=19074380; DOI=10.1128/jb.01289-08;
RA Garg S.K., Kommineni S., Henslee L., Zhang Y., Zuber P.;
RT "The YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis
RT of Spx.";
RL J. Bacteriol. 191:1268-1277(2009).
RN [4]
RP ACTIVITY REGULATION, AND INTERACTION WITH SPXO/YUZO.
RC STRAIN=168 / JH642;
RX PubMed=21378193; DOI=10.1128/jb.01350-10;
RA Kommineni S., Garg S.K., Chan C.M., Zuber P.;
RT "YjbH-enhanced proteolysis of Spx by ClpXP in Bacillus subtilis is
RT inhibited by the small protein YirB (YuzO).";
RL J. Bacteriol. 193:2133-2140(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH SPX.
RX PubMed=24942655; DOI=10.1111/mmi.12671;
RA Chan C.M., Hahn E., Zuber P.;
RT "Adaptor bypass mutations of Bacillus subtilis spx suggest a mechanism for
RT YjbH-enhanced proteolysis of the regulator Spx by ClpXP.";
RL Mol. Microbiol. 93:426-438(2014).
RN [6]
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=25353645; DOI=10.1111/mmi.12842;
RA Engman J., von Wachenfeldt C.;
RT "Regulated protein aggregation: a mechanism to control the activity of the
RT ClpXP adaptor protein YjbH.";
RL Mol. Microbiol. 95:51-63(2015).
RN [7]
RP FUNCTION, INTERACTION WITH SPX, AND 3D-STRUCTURE MODELING.
RX PubMed=27191337; DOI=10.1002/prot.25072;
RA Al-Eryani Y., Ib Rasmussen M., Kjellstroem S., Hoejrup P., Emanuelsson C.,
RA von Wachenfeldt C.;
RT "Exploring structure and interactions of the bacterial adaptor protein YjbH
RT by crosslinking mass spectrometry.";
RL Proteins 84:1234-1245(2016).
CC -!- FUNCTION: Adapter protein required for efficient degradation of Spx by
CC ClpXP under non-stress conditions (PubMed:17908206, PubMed:19074380,
CC PubMed:24942655). Interaction with Spx stabilizes Spx and exposes the
CC C-terminus of Spx for recognition and proteolysis by ClpXP
CC (PubMed:24942655, PubMed:27191337). Is specific for Spx and does not
CC enhance proteolysis by ClpCP protease (PubMed:19074380). Probably binds
CC 2 zinc ions (PubMed:19074380). {ECO:0000269|PubMed:17908206,
CC ECO:0000269|PubMed:19074380, ECO:0000269|PubMed:24942655,
CC ECO:0000269|PubMed:27191337}.
CC -!- ACTIVITY REGULATION: Irreversible aggregation upon several stress
CC conditions prevents interaction with Spx and therefore leads to Spx
CC stabilization (PubMed:25353645). Inhibited by interaction with
CC SpxO/YuzO (PubMed:21378193). {ECO:0000269|PubMed:21378193,
CC ECO:0000269|PubMed:25353645}.
CC -!- SUBUNIT: Interacts with Spx (PubMed:19074380, PubMed:24942655,
CC PubMed:27191337). Interacts with SpxO/YuzO (PubMed:21378193).
CC {ECO:0000269|PubMed:19074380, ECO:0000269|PubMed:21378193,
CC ECO:0000269|PubMed:24942655, ECO:0000269|PubMed:27191337}.
CC -!- INTERACTION:
CC O31606; O31602: spx; NbExp=3; IntAct=EBI-6406036, EBI-5248631;
CC O31606; O32302: spxO; NbExp=3; IntAct=EBI-6406036, EBI-6413973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02245,
CC ECO:0000269|PubMed:25353645}. Note=Soluble under non-stress conditions
CC and aggregates in response to stress conditions such as disulfide
CC stress, heat and ethanol. {ECO:0000269|PubMed:25353645}.
CC -!- INDUCTION: Expressed throughout cell growth. Negatively influences its
CC own expression. {ECO:0000269|PubMed:17908206}.
CC -!- DOMAIN: The histidine-rich N terminus is essential for interaction with
CC Spx. {ECO:0000269|PubMed:19074380}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene show poor growth,
CC affected sporulation, complete loss of competence development and
CC overproduce Spx under unperturbed growth. Mutants also overproduce TrxA
CC and show reduced sensitivity to disulfide stress.
CC {ECO:0000269|PubMed:17908206}.
CC -!- SIMILARITY: Belongs to the SpxH family. {ECO:0000255|HAMAP-
CC Rule:MF_02245, ECO:0000305}.
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DR EMBL; AL009126; CAB13012.2; -; Genomic_DNA.
DR PIR; H69843; H69843.
DR RefSeq; NP_389037.2; NC_000964.3.
DR RefSeq; WP_003245184.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31606; -.
DR SMR; O31606; -.
DR IntAct; O31606; 10.
DR STRING; 224308.BSU11550; -.
DR PaxDb; O31606; -.
DR PRIDE; O31606; -.
DR EnsemblBacteria; CAB13012; CAB13012; BSU_11550.
DR GeneID; 939365; -.
DR KEGG; bsu:BSU11550; -.
DR PATRIC; fig|224308.179.peg.1244; -.
DR eggNOG; COG2761; Bacteria.
DR InParanoid; O31606; -.
DR OMA; YRMGGLL; -.
DR PhylomeDB; O31606; -.
DR BioCyc; BSUB:BSU11550-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..299
FT /note="ClpXP adapter protein SpxH"
FT /id="PRO_0000278682"
FT MUTAGEN 1..24
FT /note="Missing: Eliminates Spx binding. Does not enhance
FT Spx proteolysis."
FT /evidence="ECO:0000269|PubMed:19074380"
SQ SEQUENCE 299 AA; 34422 MW; A2F4BD24A1977339 CRC64;
MTNYQHELYF AHCHGHPKKP LEIYMFVDPL CPECWSLEPV IKKLKIRYGR FFTLRIIASA
SLTALNKKRK KHLLAEAWEK IASRSGMSCD GNVWFEQDQP LSSPYMAALA FKAAELQGRK
AGMQFLRNMQ ESLFVSKKNI TDENVLLEIA ENTSLDLEEF KKDLHSQSAV KALQCDMKIA
AEMDVSVNPT LTFFNTQHED EGLKVPGSYS YDVYEEILFE MLGDEPKPSE TPPLECFIEY
FRFVASKEIA LVYDLSLEEV EKEMKKLAFA KKVAKVEAKH GMFWKSLSTY SDEYQSCEK
