ID   SRPA_SYNE7              Reviewed;         339 AA.
AC   Q55025; Q8KUU0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Catalase-related peroxidase;
DE            EC=1.11.1.-;
DE   AltName: Full=Protein SrpA;
DE   AltName: Full=Sulfur-regulated plasmid-encoded protein A;
DE   Flags: Precursor;
GN   Name=srpA; OrderedLocusNames=Synpcc7942_B2620; ORFNames=pANL46;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OG   Plasmid pANL.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-52, SUBCELLULAR
RP   LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND SIGNAL.
RC   STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RX   PubMed=7536734; DOI=10.1128/jb.177.8.2143-2150.1995;
RA   Nicholson M.L., Laudenbach D.E.;
RT   "Genes encoded on a cyanobacterial plasmid are transcriptionally regulated
RT   by sulfur availability and CysR.";
RL   J. Bacteriol. 177:2143-2150(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RX   PubMed=18353436; DOI=10.1016/j.plasmid.2008.01.005;
RA   Chen Y., Holtman C.K., Magnuson R.D., Youderian P.A., Golden S.S.;
RT   "The complete sequence and functional analysis of pANL, the large plasmid
RT   of the unicellular freshwater cyanobacterium Synechococcus elongatus PCC
RT   7942.";
RL   Plasmid 59:176-192(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of plasmid 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7536734}.
CC   -!- INDUCTION: By sulfur deprivation. {ECO:0000269|PubMed:7536734}.
CC   -!- DISRUPTION PHENOTYPE: No significant differences in the growth kinetics
CC       of cells grown in medium containing high or low concentrations of
CC       sulfate. {ECO:0000269|PubMed:7536734}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA85847.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ABB58649.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U20224; AAA85847.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF441790; AAM81171.2; -; Genomic_DNA.
DR   EMBL; CP000101; ABB58649.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_665784.2; NC_004073.2.
DR   RefSeq; WP_011055161.1; NC_007595.1.
DR   AlphaFoldDB; Q55025; -.
DR   SMR; Q55025; -.
DR   STRING; 1140.Synpcc7942_B2620; -.
DR   PeroxiBase; 6125; SeKat1.
DR   PRIDE; Q55025; -.
DR   EnsemblBacteria; ABB58649; ABB58649; Synpcc7942_B2620.
DR   KEGG; syf:Synpcc7942_B2620; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_045961_1_0_3; -.
DR   OrthoDB; 1584770at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_B2620-MON; -.
DR   GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0042743; P:hydrogen peroxide metabolic process; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08153; srpA_like; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF000296; SrpA; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Periplasm; Peroxidase; Plasmid; Signal; Stress response.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:7536734"
FT   CHAIN           32..339
FT                   /note="Catalase-related peroxidase"
FT                   /id="PRO_0000004695"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  37055 MW;  CD53DE1602528BA8 CRC64;
     MIRIRNRWFR WLAIALASLV ASIGIATVGF AATGVTPDQV LSAIEGTFGV NVGQRRNHIK
     GTCAVGNFVA TTEAKTYSRS PLFSGQSIPV VARFSLAGGN PKAPDTAKNP RGLGLQFQLP
     NNRFLNMALL NTPVFGVASP EGFYENILAI RPDPTTGKPD PEKVKAFREK YPENKAQAAF
     LASNNPPTSY ANTSYFGLHA FKFINQTNQT RLVRWQFVPQ DGEKRLTDAE LQAAPANFLE
     QKLIERTQDS PVKWDFWITL GQPGDAEDNP TIAWPSDRQQ VKVGTLTLTA ASPQPGAACE
     GINYDPLVLS DGIEPTNDPV LQFRSGVYAL SYSKRTRGL