CBBX_CERSP
ID CBBX_CERSP Reviewed; 309 AA.
AC P95648;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein CbbX;
GN Name=cbbX;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HR;
RX PubMed=9006018; DOI=10.1128/jb.179.3.663-669.1997;
RA Gibson J.L., Tabita F.R.;
RT "Analysis of the cbbXYZ operon in Rhodobacter sphaeroides.";
RL J. Bacteriol. 179:663-669(1997).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=27872295; DOI=10.1073/pnas.1610758113;
RA Loganathan N., Tsai Y.C., Mueller-Cajar O.;
RT "Characterization of the heterooligomeric red-type rubisco activase from
RT red algae.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:14019-14024(2016).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), FUNCTION, SUBUNIT, AND MUTAGENESIS
RP OF ALA-48; LYS-80; TYR-114; LYS-123; GLU-138; ARG-194; HIS-198; ARG-239;
RP SER-250; ASN-253; ARG-257 AND ARG-261.
RX PubMed=22048315; DOI=10.1038/nature10568;
RA Mueller-Cajar O., Stotz M., Wendler P., Hartl F.U., Bracher A.,
RA Hayer-Hartl M.;
RT "Structure and function of the AAA+ protein CbbX, a red-type Rubisco
RT activase.";
RL Nature 479:194-199(2011).
CC -!- FUNCTION: ATPase involved in the activation of red-type RuBisCo
CC (ribulose-1,5-bisphosphate carboxylase/oxygenase), which tends to form
CC inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP)
CC (PubMed:27872295, PubMed:22048315). Catalyzes the release of RuBP from
CC inhibited RuBisCo in an ATP-dependent manner (PubMed:27872295,
CC PubMed:22048315). Activation of RuBisCO involves the ATP-dependent
CC carboxylation of the epsilon-amino group of lysine leading to a
CC carbamate structure (PubMed:27872295, PubMed:22048315).
CC {ECO:0000269|PubMed:22048315, ECO:0000269|PubMed:27872295}.
CC -!- SUBUNIT: Forms homohexameric rings (PubMed:22048315). The oligomeric
CC transition is triggered by ribulose 1,5-biphosphate (PubMed:27872295).
CC {ECO:0000269|PubMed:22048315, ECO:0000269|PubMed:27872295}.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR EMBL; U67781; AAC44827.1; -; Genomic_DNA.
DR PDB; 3SYK; X-ray; 3.08 A; A/B=1-309.
DR PDB; 3SYL; X-ray; 3.00 A; A/B=1-309.
DR PDB; 3ZUH; EM; 21.00 A; A/B/C/D/E/F=8-296.
DR PDBsum; 3SYK; -.
DR PDBsum; 3SYL; -.
DR PDBsum; 3ZUH; -.
DR AlphaFoldDB; P95648; -.
DR SMR; P95648; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041627; AAA_lid_6.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR000470; CbxX/CfqX_mono.
DR InterPro; IPR000641; CbxX/CfxQ.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17866; AAA_lid_6; 1.
DR PRINTS; PR00819; CBXCFQXSUPER.
DR PRINTS; PR00820; CBXXCFQX.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02880; cbbX_cfxQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding.
FT CHAIN 1..309
FT /note="Protein CbbX"
FT /id="PRO_0000063034"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 48
FT /note="A->N: Reduces ATPase and activase activities 8-
FT fold."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 80
FT /note="K->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 114
FT /note="Y->A: Increases ATPase activity and abolishes
FT activase activity."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 123
FT /note="K->A: Increases ATPase activity and reduces activase
FT activity 5-fold."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 138
FT /note="E->Q: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 194
FT /note="R->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 198
FT /note="H->F: Reduces ATPase and activase activities 10-
FT fold."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 239
FT /note="R->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 250
FT /note="S->D: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 253
FT /note="N->D: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 257
FT /note="R->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT MUTAGEN 261
FT /note="R->A: Abolishes ATPase and activase activities."
FT /evidence="ECO:0000269|PubMed:22048315"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 37..59
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3SYK"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:3SYL"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:3SYL"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 247..268
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:3SYL"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3SYK"
SQ SEQUENCE 309 AA; 34684 MW; A0F719C798C360AB CRC64;
MTDAATAPTS IDLRAEYEGS GAKEVLEELD RELIGLKPVK DRIRETAALL LVERARQKLG
LAHETPTLHM SFTGNPGTGK TTVALKMAGL LHRLGYVRKG HLVSVTRDDL VGQYIGHTAP
KTKEVLKRAM GGVLFIDEAY YLYRPDNERD YGQEAIEILL QVMENNRDDL VVILAGYADR
MENFFQSNPG FRSRIAHHIE FPDYSDEELF EIAGHMLDDQ NYQMTPEAET ALRAYIGLRR
NQPHFANARS IRNALDRARL RQANRLFTAS SGPLDARALS TMAEEDIRAS RVFKGGLDSE
RRAAEALAR
