ID   RBLL_BORBR              Reviewed;         423 AA.
AC   Q7WNK2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Uncharacterized ribulose bisphosphate carboxylase-like protein;
DE            Short=RuBisCO-like protein;
GN   OrderedLocusNames=BB1035;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: May be involved in sulfur metabolism and oxidative stress
CC       response. Does not show RuBisCO activity (By similarity).
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type IV
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BX640440; CAE31534.1; -; Genomic_DNA.
DR   RefSeq; WP_010926029.1; NC_002927.3.
DR   AlphaFoldDB; Q7WNK2; -.
DR   SMR; Q7WNK2; -.
DR   KEGG; bbr:BB1035; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_0_4; -.
DR   Proteomes; UP000001027; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   CDD; cd08207; RLP_NonPhot; 1.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding.
FT   CHAIN           1..423
FT                   /note="Uncharacterized ribulose bisphosphate carboxylase-
FT                   like protein"
FT                   /id="PRO_0000062684"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT   MOD_RES         181
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
SQ   SEQUENCE   423 AA;  45188 MW;  5F8CAB5F4935BECF CRC64;
     MSDRFEATYL IETPHDVASV AQELAGEQST ATSSRMPGET DALIRDFGAR VEHIEALPPA
     EAPSLPVAHT LGQRVHRARL TLSWPLHNIG DSLPMLLTTL LGNQTGMRRL SGIRLERVAM
     PQSFIAAQPR PAFGIAGTRR LTGVQGRPLI GSIVKPNIGL APEQTAAMAR QLAEGGVDFI
     KDDELLANPP YSPVARRAAL VLRALDEAAQ RTGRRTMYAV NITDGLDEMR RHHDAVVQAG
     GTCIMVNLNS VGLSALLALR RHSQLPIHGH RAGWAMMTRC PALGMEFQPY QMLHRLAGVD
     HLHVSGLGGK FWEHADSVLQ AAHECLTPLD TQAGAADDRA LPVFSGGSTI FDVAPTYQGI
     GTADLIFASG GGIFGHPDGL AAGCASLRQA WEAAIAGQEL RAYAQSRPEL AAALARGKPV
     RKA
//