ID   CPCS_SYNP2              Reviewed;         198 AA.
AC   A8HTM2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Phycocyanobilin lyase subunit CpcS;
DE            EC=4.-.-.-;
GN   Name=cpcS; Synonyms=cpcS-I; OrderedLocusNames=SYNPCC7002_A1822;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], POSSIBLE SUBUNIT, FUNCTION IN
RP   CHROMOPHORE ATTACHMENT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX   PubMed=18199754; DOI=10.1074/jbc.m708164200;
RA   Shen G., Schluchter W.M., Bryant D.A.;
RT   "Biogenesis of phycobiliproteins: I. cpcS-I and cpcU mutants of the
RT   cyanobacterium Synechococcus sp. PCC 7002 define a heterodimeric
RT   phyococyanobilin lyase specific for beta-phycocyanin and allophycocyanin
RT   subunits.";
RL   J. Biol. Chem. 283:7503-7512(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION IN CHROMOPHORE ATTACHMENT, AND INTERACTION WITH CPCU.
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX   PubMed=18199753; DOI=10.1074/jbc.m708165200;
RA   Saunee N.A., Williams S.R., Bryant D.A., Schluchter W.M.;
RT   "Biogenesis of phycobiliproteins: II. CpcS-I and CpcU comprise the
RT   heterodimeric bilin lyase that attaches phycocyanobilin to Cys-82 of beta-
RT   phycocyanin and CYS-81 of allophycocyanin subunits in Synechococcus sp. PCC
RT   7002.";
RL   J. Biol. Chem. 283:7513-7522(2008).
RN   [4]
RP   PROTEIN SUBSTRATES, AND INTERACTION WITH CPCU.
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX   PubMed=20228104; DOI=10.1128/aem.03100-09;
RA   Biswas A., Vasquez Y.M., Dragomani T.M., Kronfel M.L., Williams S.R.,
RA   Alvey R.M., Bryant D.A., Schluchter W.M.;
RT   "Biosynthesis of cyanobacterial phycobiliproteins in Escherichia coli:
RT   chromophorylation efficiency and specificity of all bilin lyases from
RT   Synechococcus sp. strain PCC 7002.";
RL   Appl. Environ. Microbiol. 76:2729-2739(2010).
CC   -!- FUNCTION: Attaches a phycocyanobilin (PCB) chromophore to 'Cys-82' of
CC       the C-phycocyanain beta subunit (PhcB) and the unique PCB that is
CC       attached to allophycocyanin alpha and beta subunits (ApcA and ApcB). In
CC       vitro, and probably also in vivo, chromophorylates ApcD and ApcF.
CC       {ECO:0000269|PubMed:18199753, ECO:0000269|PubMed:18199754}.
CC   -!- SUBUNIT: Forms a heterodimer with CpcU.
CC   -!- DISRUPTION PHENOTYPE: Cells are a yellow color, 70% reduction in
CC       phycobiliproteins, grow slowly, have an increased sensitivity to high
CC       light and a long lag phase. The C-phycocyanin beta subunit (PhcB) in
CC       this strain is missing the phycocyanobilin chromophore on 'Cys-82'.
CC       {ECO:0000269|PubMed:18199754}.
CC   -!- SIMILARITY: Belongs to the CpcS/CpeS biliprotein lyase family.
CC       {ECO:0000305}.
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DR   EMBL; EU145731; ABV80281.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACA99810.1; -; Genomic_DNA.
DR   RefSeq; WP_012307433.1; NC_010475.1.
DR   AlphaFoldDB; A8HTM2; -.
DR   SMR; A8HTM2; -.
DR   STRING; 32049.SYNPCC7002_A1822; -.
DR   EnsemblBacteria; ACA99810; ACA99810; SYNPCC7002_A1822.
DR   KEGG; syp:SYNPCC7002_A1822; -.
DR   eggNOG; ENOG502Z8E6; Bacteria.
DR   HOGENOM; CLU_096258_0_0_3; -.
DR   OMA; LWFASPN; -.
DR   BRENDA; 4.4.1.29; 6187.
DR   Proteomes; UP000001688; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017009; P:protein-phycocyanobilin linkage; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..198
FT                   /note="Phycocyanobilin lyase subunit CpcS"
FT                   /id="PRO_0000403139"
SQ   SEQUENCE   198 AA;  22525 MW;  7FC3D3BC3300C849 CRC64;
     MQSFADAKEF FQYSAGQWQS RRVTHHLPFR RAESGGSNIQ VETLEKDDPR IIEICQMHDM
     DASLSVGGSY VTWAGTMQWD KDDENHEGST VFALIPDADN PRQGKLLRER GYAEIVPVAG
     EYHLDHEDGL VLTTEYETMT IYERFWFANP DLRLRTSTVK RFGGFNTTTF CMEERIQTSP
     VTATAAAETN PLYAISGW