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 27-MAR-2024, entry version 133. 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 ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OG Plasmid pANL. OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC 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=ATCC 33912 / 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=ATCC 33912 / 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=ATCC 33912 / 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., Golden S., 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; NZ_JACJTX010000007.1. DR AlphaFoldDB; Q55025; -. DR SMR; Q55025; -. DR PeroxiBase; 6125; SeKat1. DR PaxDb; 1140-Synpcc7942_B2620; -. DR GeneID; 76401362; -. DR KEGG; syf:Synpcc7942_B2620; -. DR eggNOG; COG0753; Bacteria. DR HOGENOM; CLU_045961_1_0_3; -. DR OrthoDB; 255727at2; -. DR BioCyc; SYNEL:SYNPCC7942_B2620-MONOMER; -. DR Proteomes; UP000889800; Plasmid pANL. 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 Gene3D; 1.20.1280.120; -; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1. DR PANTHER; PTHR11465:SF9; CATALASE; 1. DR Pfam; PF00199; Catalase; 1. DR PIRSF; PIRSF000296; SrpA; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF56634; Heme-dependent catalase-like; 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; Reference proteome; Signal; KW 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 //