SPXH_GEOKA
ID SPXH_GEOKA Reviewed; 297 AA.
AC Q5L1S1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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:30982633}; OrderedLocusNames=GK0824;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2] {ECO:0007744|PDB:6GHB, ECO:0007744|PDB:6GHO}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEXES WITH B.SUBTILIS SPX,
RP FUNCTION, SUBUNIT, INTERACTION WITH SPX, DOMAIN, AND MUTAGENESIS OF GLU-27;
RP GLU-164 AND ASP-168.
RX PubMed=30982633; DOI=10.1016/j.str.2019.03.009;
RA Awad W., Al-Eryani Y., Ekstrom S., Logan D.T., von Wachenfeldt C.;
RT "Structural basis for YjbH adaptor-mediated recognition of transcription
RT factor Spx.";
RL Structure 27:923-936.e6(2019).
CC -!- FUNCTION: Adapter protein required for efficient degradation of Spx by
CC ClpXP under non-stress conditions (By similarity). Interaction with Spx
CC stabilizes Spx and exposes the C-terminus of Spx for recognition and
CC proteolysis by ClpXP (PubMed:30982633). {ECO:0000250|UniProtKB:O31606,
CC ECO:0000269|PubMed:30982633}.
CC -!- SUBUNIT: Monomer (PubMed:30982633). Interacts with Spx
CC (PubMed:30982633). {ECO:0000269|PubMed:30982633}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02245}.
CC -!- DOMAIN: Contains a DsbA-like thioredoxin domain connected via a linker
CC to a C-terminal domain reminiscent of the winged helix-turn-helix fold.
CC {ECO:0000269|PubMed:30982633}.
CC -!- SIMILARITY: Belongs to the SpxH family. {ECO:0000255|HAMAP-
CC Rule:MF_02245}.
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DR EMBL; BA000043; BAD75109.1; -; Genomic_DNA.
DR RefSeq; WP_011230325.1; NC_006510.1.
DR PDB; 6GHB; X-ray; 3.10 A; B/D=1-297.
DR PDB; 6GHO; X-ray; 1.79 A; B=1-297.
DR PDBsum; 6GHB; -.
DR PDBsum; 6GHO; -.
DR AlphaFoldDB; Q5L1S1; -.
DR SMR; Q5L1S1; -.
DR STRING; 235909.GK0824; -.
DR EnsemblBacteria; BAD75109; BAD75109; GK0824.
DR KEGG; gka:GK0824; -.
DR eggNOG; COG2761; Bacteria.
DR HOGENOM; CLU_069785_0_0_9; -.
DR OMA; YRMGGLL; -.
DR Proteomes; UP000001172; 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 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..297
FT /note="ClpXP adapter protein SpxH"
FT /id="PRO_0000278683"
FT MUTAGEN 27
FT /note="E->A: Decreases interaction with Spx."
FT /evidence="ECO:0000269|PubMed:30982633"
FT MUTAGEN 164
FT /note="E->A: Decreases interaction with Spx."
FT /evidence="ECO:0000269|PubMed:30982633"
FT MUTAGEN 168
FT /note="D->A: Decreases interaction with Spx."
FT /evidence="ECO:0000269|PubMed:30982633"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6GHO"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:6GHO"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:6GHO"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:6GHO"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:6GHO"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:6GHO"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:6GHO"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:6GHO"
SQ SEQUENCE 297 AA; 33591 MW; 48C2D602BCEBB05E CRC64;
MSEKFAGKTT STCYPSQPLG NTNKPLELYL FIDPLCPECW GLEPVIKKLT IEYGRFFTLR
HILSGTWATW SARKGTKPEA MAKAWEWAAN RTGMSCDGSV WLENPISSPF APSLAIKAAE
MQGKRAGLRF LRKLQEQLFL EKQNVADLSV LAECAVKAGL DVDEFLRDMH SPGAAKAFQC
DLKITSEMDV DEIPTLVLFN ENIEDEGIKI SGCYPYDIYV ELIAEMLGFH PEPSSPPPLE
SFLSHFKFVA TKEVAVVYNW TIQEAETEMK KLQLKQKVER VPVKHGTFWR YIDDSRP
