ID   CPES_PROMP              Reviewed;         183 AA.
AC   Q7V2Z2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Phycoerythrobilin lyase CpeS;
DE            EC=4.-.-.-;
GN   Name=cpeS; OrderedLocusNames=PMM0306;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
RN   [2]
RP   FUNCTION AS A CHROMOPHORE LYASE, CHROMOPHORE-BINDING, AND SUBUNIT.
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=20876568; DOI=10.1074/jbc.m110.172619;
RA   Wiethaus J., Busch A.W., Kock K., Leichert L.I., Herrmann C.,
RA   Frankenberg-Dinkel N.;
RT   "CpeS is a lyase specific for attachment of 3Z-PEB to Cys82 of {beta}-
RT   phycoerythrin from Prochlorococcus marinus MED4.";
RL   J. Biol. Chem. 285:37561-37569(2010).
CC   -!- FUNCTION: Acts as a chromphore lyase, covalently attaching 3Z-
CC       phycoerythrobilin (3Z-PEB) to its target protein CpeB (phycoerythrin).
CC       Binds the isomeric chromophores 3E-phycoerythrobilin (3E-PEB), 3Z-PEB
CC       as well as their precursor 15,16-dihydrobiliverdin (DHBV) but not other
CC       chromophores tested. While it can transfer 3E-PEB a non-physiological
CC       adduct is made. Chromophore is bound to the lyase in a ratio of nearly
CC       1:1. {ECO:0000269|PubMed:20876568}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20876568}.
CC   -!- SIMILARITY: Belongs to the CpcS/CpeS biliprotein lyase family.
CC       {ECO:0000305}.
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DR   EMBL; BX548174; CAE18765.1; -; Genomic_DNA.
DR   RefSeq; WP_011131943.1; NC_005072.1.
DR   AlphaFoldDB; Q7V2Z2; -.
DR   SMR; Q7V2Z2; -.
DR   STRING; 59919.PMM0306; -.
DR   EnsemblBacteria; CAE18765; CAE18765; PMM0306.
DR   KEGG; pmm:PMM0306; -.
DR   eggNOG; ENOG503229I; Bacteria.
DR   HOGENOM; CLU_096258_0_0_3; -.
DR   OMA; ERIWFVS; -.
DR   OrthoDB; 1672344at2; -.
DR   BioCyc; MetaCyc:TX50_RS01585-MON; -.
DR   BRENDA; 4.4.1.29; 12279.
DR   Proteomes; UP000001026; 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   1: Evidence at protein level;
KW   Lyase.
FT   CHAIN           1..183
FT                   /note="Phycoerythrobilin lyase CpeS"
FT                   /id="PRO_0000403138"
SQ   SEQUENCE   183 AA;  21154 MW;  CB4F6C6A316EDD02 CRC64;
     MTKNLITINQ FIQKSLGEWK SIRSTHSLAF QEVENSTSKI EIKELESNNK NVLGLLEKYN
     YTSKPSFIAL SISWKAISDW EIDQKIEQDK TILLFLPKDK NKGIVLRNKG YTESVISSSE
     YLIDENENLN IKTIYSSTAS EERICFLSNH IRSRYSVIRN NENNTVIQTS HTSEIRNMSI
     LKD