CPCS2_NOSS1
ID CPCS2_NOSS1 Reviewed; 180 AA.
AC Q8YLK6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Putative phycocyanobilin lyase CpcS 2;
DE EC=4.-.-.-;
GN Name=cpeS2; OrderedLocusNames=all5292;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP INDUCTION, FUNCTION, AND LACK OF CHROMOPHORE LYASE ACTIVITY IN VITRO.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=17895251; DOI=10.1074/jbc.m703038200;
RA Zhao K.H., Zhang J., Tu J.M., Bohm S., Ploscher M., Eichacker L.,
RA Bubenzer C., Scheer H., Wang X., Zhou M.;
RT "Lyase activities of CpcS- and CpcT-like proteins from Nostoc PCC7120 and
RT sequential reconstitution of binding sites of phycoerythrocyanin and
RT phycocyanin beta-subunits.";
RL J. Biol. Chem. 282:34093-34103(2007).
RN [3]
RP FUNCTION, AND LACK OF CHROMOPHORE LYASE ACTIVITY IN VITRO.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=17726096; DOI=10.1073/pnas.0706209104;
RA Zhao K.H., Su P., Tu J.M., Wang X., Liu H., Ploscher M., Eichacker L.,
RA Yang B., Zhou M., Scheer H.;
RT "Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for
RT cysteine-84-binding sites in cyanobacterial phycobiliproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14300-14305(2007).
CC -!- FUNCTION: Covalently attaches a chromophore to Cys residue(s) of
CC phycobiliproteins (Potential). In vitro does not act as a chromophore
CC lyase for ApcA1, ApcA2, ApcB, ApcD, ApcF, CpcB or PecB, the lyase
CC activity is therefore unsure. {ECO:0000269|PubMed:17726096,
CC ECO:0000269|PubMed:17895251, ECO:0000305}.
CC -!- INDUCTION: Induced by nitrogen starvation.
CC {ECO:0000269|PubMed:17895251}.
CC -!- SIMILARITY: Belongs to the CpcS/CpeS biliprotein lyase family.
CC {ECO:0000305}.
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DR EMBL; BA000019; BAB76991.1; -; Genomic_DNA.
DR PIR; AD2467; AD2467.
DR RefSeq; WP_010999416.1; NZ_RSCN01000005.1.
DR AlphaFoldDB; Q8YLK6; -.
DR SMR; Q8YLK6; -.
DR STRING; 103690.17134431; -.
DR EnsemblBacteria; BAB76991; BAB76991; BAB76991.
DR KEGG; ana:all5292; -.
DR eggNOG; ENOG5030ATU; Bacteria.
DR OMA; QLMIGQY; -.
DR OrthoDB; 1565411at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017009; P:protein-phycocyanobilin linkage; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR HAMAP; MF_01459; Chrphore_lyase_CpxS; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR018536; CpcS/CpeS.
DR Pfam; PF09367; CpeS; 1.
PE 2: Evidence at transcript level;
KW Lyase; Reference proteome.
FT CHAIN 1..180
FT /note="Putative phycocyanobilin lyase CpcS 2"
FT /id="PRO_0000403137"
SQ SEQUENCE 180 AA; 20661 MW; 506D12AB978746E7 CRC64;
MKSLSKLVRT VDESQIIEFF QESVGEWCSQ RRYYTLPDGE TKEMMSMITI RFLEQGCDEL
QKLAQIHKLA ESVFLICGAE VTWCSTDVLK NRSESEGSTL FGALGNILYR DRGFATSKPV
TAQYNFPNPK TLCLRTEYNG SVFEEELKLI GSKYRTRQTI ISRAGEQLMI GQYIEKRIVQ