ID   BSSE_THAAR              Reviewed;         286 AA.
AC   Q8VVE4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Putative chaperone BssE;
GN   Name=bssE;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=9632263; DOI=10.1046/j.1365-2958.1998.00826.x;
RA   Leuthner B., Leutwein C., Schulz H., Horth P., Haehnel W., Schiltz E.,
RA   Schagger H., Heider J.;
RT   "Biochemical and genetic characterization of benzylsuccinate synthase from
RT   Thauera aromatica: a new glycyl radical enzyme catalysing the first step in
RT   anaerobic toluene metabolism.";
RL   Mol. Microbiol. 28:615-628(1998).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=11807562; DOI=10.1007/s00203-001-0375-1;
RA   Hermuth K., Leuthner B., Heider J.;
RT   "Operon structure and expression of the genes for benzylsuccinate synthase
RT   in Thauera aromatica strain K172.";
RL   Arch. Microbiol. 177:132-138(2002).
CC   -!- FUNCTION: May have a role in assembly and/or activation of
CC       benzylsuccinate synthase. {ECO:0000269|PubMed:11807562}.
CC   -!- INDUCTION: Induced by toluene. {ECO:0000269|PubMed:11807562}.
CC   -!- SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family. {ECO:0000305}.
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DR   EMBL; AJ001848; CAD12889.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VVE4; -.
DR   SMR; Q8VVE4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR013615; CbbQ_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF07728; AAA_5; 1.
DR   Pfam; PF08406; CbbQ_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; ATP-binding; Chaperone;
KW   Nucleotide-binding.
FT   CHAIN           1..286
FT                   /note="Putative chaperone BssE"
FT                   /id="PRO_0000418877"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   286 AA;  31721 MW;  2CFBD8887BE7AC0F CRC64;
     MKNSGLLNSV HVPAADPYYY LNTETLSLLN RIQRISQKHP VNVLVIGKQG CGKSSLVRQY
     AAVHHLPLAT FQIGLLSEPG QLFGEYALEN GETRYKQFLF PQAIQTPGCV IHLEEINRPE
     HPKALNMLFS ILSDDRQVWM DELGLLKVAD GVVFFATLNE GDEFVGTELL DPALRDRFYV
     TAMDFLPNDV EREVLQKKTG VTIAQAEEII GVVNSLRASP ELGVEVSTRK TLMIGEMIAA
     GGSLREAIAA SLQTDRETLE SVLLSLHVEL GKTERGTTEY VLFTPR