RBLL_CHLTE
ID RBLL_CHLTE Reviewed; 435 AA.
AC Q8KBL4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ribulose bisphosphate carboxylase-like protein;
DE Short=RuBisCO-like protein;
GN OrderedLocusNames=CT1772;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [2] {ECO:0000305}
RP FUNCTION.
RC STRAIN=WT2321 {ECO:0000269|PubMed:11287671};
RX PubMed=11287671; DOI=10.1073/pnas.081610398;
RA Hanson T.E., Tabita F.R.;
RT "A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein
RT from Chlorobium tepidum that is involved with sulfur metabolism and the
RT response to oxidative stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4397-4402(2001).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, AND SUBUNIT.
RC STRAIN=WT2321 {ECO:0000269|PubMed:15893668};
RX PubMed=15893668; DOI=10.1016/j.str.2005.02.017;
RA Li H., Sawaya M.R., Tabita F.R., Eisenberg D.;
RT "Crystal structure of a RuBisCO-like protein from the green sulfur
RT bacterium Chlorobium tepidum.";
RL Structure 13:779-789(2005).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RA Fedorov A.A., Fedorov E.V., Imker H.J., Gerlt J.A., Almo S.C.;
RT "Crystal structure of a RuBisCO-like protein from Chlorobium tepidum.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: May be involved in sulfur metabolism and oxidative stress
CC response. Does not show RuBisCO activity. {ECO:0000269|PubMed:11287671,
CC ECO:0000269|PubMed:15893668}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15893668}.
CC -!- INTERACTION:
CC Q8KBL4; Q8KBL4: CT1772; NbExp=2; IntAct=EBI-15552219, EBI-15552219;
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Although strongly related to RuBisCO family, it lacks the
CC conserved Lys active site in position 327, which is replaced by an Arg
CC residue, suggesting that it may catalyze enolization but not
CC carboxylation. {ECO:0000305}.
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DR EMBL; AE006470; AAM72993.1; -; Genomic_DNA.
DR RefSeq; NP_662651.1; NC_002932.3.
DR RefSeq; WP_010933432.1; NC_002932.3.
DR PDB; 1TEL; X-ray; 2.70 A; A/B=1-435.
DR PDB; 1YKW; X-ray; 2.00 A; A/B=1-435.
DR PDBsum; 1TEL; -.
DR PDBsum; 1YKW; -.
DR AlphaFoldDB; Q8KBL4; -.
DR SMR; Q8KBL4; -.
DR DIP; DIP-48441N; -.
DR STRING; 194439.CT1772; -.
DR EnsemblBacteria; AAM72993; AAM72993; CT1772.
DR KEGG; cte:CT1772; -.
DR PATRIC; fig|194439.7.peg.1606; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_10; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR EvolutionaryTrace; Q8KBL4; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..435
FT /note="Ribulose bisphosphate carboxylase-like protein"
FT /id="PRO_0000062679"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 198
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1YKW"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1YKW"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 332..343
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1YKW"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1YKW"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 412..416
FT /evidence="ECO:0007829|PDB:1YKW"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:1YKW"
SQ SEQUENCE 435 AA; 48003 MW; 41C282555ED2ECB0 CRC64;
MNAEDVKGFF ASRESLDMEQ YLVLDYYLES VGDIETALAH FCSEQSTAQW KRVGVDEDFR
LVHAAKVIDY EVIEELEQLS YPVKHSETGK IHACRVTIAH PHCNFGPKIP NLLTAVCGEG
TYFTPGVPVV KLMDIHFPDT YLADFEGPKF GIEGLRDILN AHGRPIFFGV VKPNIGLSPG
EFAEIAYQSW LGGLDIAKDD EMLADVTWSS IEERAAHLGK ARRKAEAETG EPKIYLANIT
DEVDSLMEKH DVAVRNGANA LLINALPVGL SAVRMLSNYT QVPLIGHFPF IASFSRMEKY
GIHSKVMTKL QRLAGLDAVI MPGFGDRMMT PEEEVLENVI ECTKPMGRIK PCLPVPGGSD
SALTLQTVYE KVGNVDFGFV PGRGVFGHPM GPKAGAKSIR QAWEAIEQGI SIETWAETHP
ELQAMVDQSL LKKQD
