ID   A0A380G8Z5_STAIN        Unreviewed;       408 AA.
AC   A0A380G8Z5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Deferrochelatase {ECO:0000256|ARBA:ARBA00033771, ECO:0000256|RuleBase:RU365017};
DE            EC=1.11.1.- {ECO:0000256|RuleBase:RU365017};
DE   AltName: Full=Peroxidase EfeB {ECO:0000256|ARBA:ARBA00033775, ECO:0000256|RuleBase:RU365017};
GN   Name=efeN {ECO:0000313|EMBL:SUM47619.1};
GN   ORFNames=NCTC11048_02704 {ECO:0000313|EMBL:SUM47619.1};
OS   Staphylococcus intermedius NCTC 11048.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus; Staphylococcus intermedius group.
OX   NCBI_TaxID=1141106 {ECO:0000313|EMBL:SUM47619.1, ECO:0000313|Proteomes:UP000255549};
RN   [1] {ECO:0000313|EMBL:SUM47619.1, ECO:0000313|Proteomes:UP000255549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11048 {ECO:0000313|Proteomes:UP000255549};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the recovery of exogenous heme iron. Extracts
CC       iron from heme while preserving the protoporphyrin ring intact.
CC       {ECO:0000256|RuleBase:RU365017}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC         Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.98.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00034258};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585;
CC         Evidence={ECO:0000256|ARBA:ARBA00034258};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|RuleBase:RU365017};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC       per subunit. {ECO:0000256|RuleBase:RU365017};
CC   -!- SIMILARITY: Belongs to the DyP-type peroxidase family.
CC       {ECO:0000256|RuleBase:RU365017}.
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DR   EMBL; UHDP01000003; SUM47619.1; -; Genomic_DNA.
DR   RefSeq; WP_019167346.1; NZ_UHDP01000003.1.
DR   AlphaFoldDB; A0A380G8Z5; -.
DR   STRING; 1141106.GCA_000308095_02503; -.
DR   OrthoDB; 9781066at2; -.
DR   Proteomes; UP000255549; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:RHEA.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033212; P:iron import into cell; IEA:InterPro.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR048328; Dyp_perox_C.
DR   InterPro; IPR048327; Dyp_perox_N.
DR   InterPro; IPR006314; Dyp_peroxidase.
DR   InterPro; IPR006313; EfeB/EfeN.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01413; Dyp_perox_fam; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   NCBIfam; TIGR01412; tat_substr_1; 1.
DR   PANTHER; PTHR30521:SF4; DEFERROCHELATASE; 1.
DR   PANTHER; PTHR30521; DEFERROCHELATASE/PEROXIDASE; 1.
DR   Pfam; PF20628; Dyp_perox_C; 1.
DR   Pfam; PF04261; Dyp_perox_N; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR   PROSITE; PS51404; DYP_PEROXIDASE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU365017};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365017};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365017};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU365017};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU365017};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..214
FT                   /note="Dyp-type peroxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04261"
FT   DOMAIN          222..397
FT                   /note="Dyp-type peroxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20628"
SQ   SEQUENCE   408 AA;  45520 MW;  3F8089B548C93AB6 CRC64;
     MTQENNHHET TYSRRSFLKM LGVGGAGVAI GASGVGSIFS FKSMFDTPQE DSDQAYQFYG
     KVQPGITTPT QKNINLVVLD LKSKDKTTVQ KMFRAWTEST VKMMHGEAIG KTTSNTLLPP
     IDTGEAIGLD ANKLTITFGV SKDFLQKLGL NGKIPKSFKD LPHFPNDQLD KDITGGDIFI
     QACADDPQVA FHAIHNLIRP YLDVVQVKWS ETGFISGKGK ETPRNLMAFK DGTQNPRDTK
     GYKDYVFLED GWAKYGTYCV LRKIQIHIET WDRTALEEQE ATFGRHRASG APLGKKDEFD
     EMDLSAKDAH GEYVIPKDAH ARLAKEANTE ILRRAYNYMR GTNDKTGNYD AGLLFISFQK
     HPQQFIDIQN NLGSVDKLNE YITHKGSGLF LILPGVKKGG YLGETLFN
//