ID   A0A380G8Z5_STAIN        Unreviewed;       408 AA.
AC   A0A380G8Z5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-FEB-2019, entry version 4.
DE   RecName: Full=Deferrochelatase/peroxidase {ECO:0000256|RuleBase:RU365017};
DE            EC=1.11.1.- {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; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
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.
CC       Extracts iron from heme while preserving the tetrapyrrol ring
CC       intact. {ECO:0000256|RuleBase:RU365017}.
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-
CC       covalently 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   Proteomes; UP000255549; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR006314; Dyp_peroxidase.
DR   InterPro; IPR006313; EfeB.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF04261; Dyp_perox; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   TIGRFAMs; TIGR01412; tat_substr_1; 1.
DR   PROSITE; PS51404; DYP_PEROXIDASE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000255549};
KW   Heme {ECO:0000256|RuleBase:RU365017};
KW   Iron {ECO:0000256|RuleBase:RU365017};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU365017};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU365017,
KW   ECO:0000313|EMBL:SUM47619.1};
KW   Peroxidase {ECO:0000256|RuleBase:RU365017,
KW   ECO:0000313|EMBL:SUM47619.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     21     41       Helical. {ECO:0000256|SAM:Phobius}.
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
//