ID   SSPB_HAEIN              Reviewed;         150 AA.
AC   P45206;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Stringent starvation protein B homolog;
DE   AltName: Full=Adapter protein SspB;
DE   AltName: Full=Specificity-enhancing factor SspB;
GN   Name=sspB; OrderedLocusNames=HI_1440;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Enhances recognition of ssrA-tagged proteins by the ClpX-ClpP
CC       protease; the ssrA degradation tag (AANDENYALAA) is added trans-
CC       translationally to proteins that are stalled on the ribosome, freeing
CC       the ribosome and targeting stalled peptides for degradation. SspB
CC       activates the ATPase activity of ClpX. Seems to act in concert with
CC       SspA in the regulation of several proteins during exponential and
CC       stationary-phase growth (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Also stimulates degradation of the N-terminus of RseA
CC       (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in a
CC       non-ssrA-mediated fashion. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SspB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L42023; AAC23089.1; -; Genomic_DNA.
DR   PIR; D64123; D64123.
DR   RefSeq; NP_439592.1; NC_000907.1.
DR   RefSeq; WP_005650453.1; NC_000907.1.
DR   PDB; 1OU8; X-ray; 1.60 A; A/B=1-111.
DR   PDB; 1OU9; X-ray; 1.80 A; A/B/C=1-129.
DR   PDB; 1OUL; X-ray; 2.20 A; A/B=1-129.
DR   PDB; 1TWB; X-ray; 1.90 A; A/B=1-110.
DR   PDB; 1ZSZ; X-ray; 2.00 A; A=1-110, B=1-111, C=1-129.
DR   PDBsum; 1OU8; -.
DR   PDBsum; 1OU9; -.
DR   PDBsum; 1OUL; -.
DR   PDBsum; 1TWB; -.
DR   PDBsum; 1ZSZ; -.
DR   AlphaFoldDB; P45206; -.
DR   SMR; P45206; -.
DR   STRING; 71421.HI_1440; -.
DR   EnsemblBacteria; AAC23089; AAC23089; HI_1440.
DR   KEGG; hin:HI_1440; -.
DR   PATRIC; fig|71421.8.peg.1502; -.
DR   eggNOG; COG2969; Bacteria.
DR   HOGENOM; CLU_118425_0_0_6; -.
DR   OMA; FQARFGG; -.
DR   PhylomeDB; P45206; -.
DR   BioCyc; HINF71421:G1GJ1-1466-MON; -.
DR   EvolutionaryTrace; P45206; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR   Gene3D; 2.30.30.220; -; 1.
DR   InterPro; IPR007481; SspB.
DR   InterPro; IPR036760; SspB-like_sf.
DR   PANTHER; PTHR37486; PTHR37486; 1.
DR   Pfam; PF04386; SspB; 1.
DR   PIRSF; PIRSF005276; SspB; 1.
DR   SUPFAM; SSF101738; SSF101738; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome.
FT   CHAIN           1..150
FT                   /note="Stringent starvation protein B homolog"
FT                   /id="PRO_0000072220"
FT   REGION          114..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           9..22
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1OUL"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1OUL"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          66..75
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          78..85
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:1OU8"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:1OU8"
SQ   SEQUENCE   150 AA;  17168 MW;  E8A2E3BD550732A1 CRC64;
     MEYKSSPKRP YLLRAYYDWL VDNSFTPYLV VDATYLGVNV PVEYVKDGQI VLNLSASATG
     NLQLTNDFIQ FNARFKGVSR ELYIPMGAAL AIYARENGDG VMFEPEEIYD ELNIEPDTEQ
     PTGFYEAVDK PKKREEKKKT KSVSHLRIVD