HEMTB_CAMJ8
ID HEMTB_CAMJ8 Reviewed; 133 AA.
AC A8FK31;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Bacteriohemerythrin {ECO:0000255|HAMAP-Rule:MF_00556};
GN OrderedLocusNames=C8J_0219;
OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS 11828).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=407148;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81116 / NCTC 11828;
RX PubMed=17873037; DOI=10.1128/jb.01404-07;
RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA van Vliet A.H.M.;
RT "The complete genome sequence of Campylobacter jejuni strain 81116
RT (NCTC11828).";
RL J. Bacteriol. 189:8402-8403(2007).
CC -!- FUNCTION: Oxygen-binding protein. May be involved in a storage
CC mechanism or for delivery to oxygen-requiring enzymes. The oxygen-
CC binding site contains two iron atoms. {ECO:0000255|HAMAP-
CC Rule:MF_00556}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00556}.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000255|HAMAP-
CC Rule:MF_00556}.
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DR EMBL; CP000814; ABV51818.1; -; Genomic_DNA.
DR RefSeq; WP_002851900.1; NC_009839.1.
DR AlphaFoldDB; A8FK31; -.
DR SMR; A8FK31; -.
DR KEGG; cju:C8J_0219; -.
DR HOGENOM; CLU_086902_3_2_7; -.
DR OMA; ETPNAIY; -.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; -; 1.
DR HAMAP; MF_00556; Hemerythrin; 1.
DR InterPro; IPR023504; Bacteriohemerythrin-like.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR Pfam; PF01814; Hemerythrin; 1.
DR SUPFAM; SSF47188; SSF47188; 1.
DR TIGRFAMs; TIGR02481; hemeryth_dom; 1.
DR PROSITE; PS00550; HEMERYTHRINS; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..133
FT /note="Bacteriohemerythrin"
FT /id="PRO_1000072561"
FT BINDING 19
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00556"
SQ SEQUENCE 133 AA; 16189 MW; 1862870B17744C24 CRC64;
MTYNEKIISM NNDLLDHQHK ELFEISKKLS LMNQRHVGTK ELKIVLRELL IMINRHFSDE
EAFMREIEYP YINHHTRIHR KIILEIEEII ISEAKFVNIM TEKLNLVVQD FIFKHTAKED
SKIVKYYEEK FKK
