ID   HEMWL_BUCBP             Reviewed;         374 AA.
AC   Q89A47;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Putative heme chaperone HemW-like protein;
GN   Name=hemW {ECO:0000250|UniProtKB:P52062}; OrderedLocusNames=bbp_498;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: Might be a heme chaperone; in E.coli heme binds independently
CC       of binding to [4Fe-4S] or S-adenosyl-L-methionine.
CC       {ECO:0000250|UniProtKB:P52062, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CGF7}.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC       family. HemW subfamily. {ECO:0000305}.
CC   -!- CAUTION: Pro-13, Tyr-17 and His-20 are present instead of the conserved
CC       Cys which are required to bind a 4Fe-4S-S-AdoMet cluster, as occurs
CC       with other proteins of this family. This protein may be an inactive
CC       homolog. {ECO:0000305}.
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DR   EMBL; AE016826; AAO27203.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q89A47; -.
DR   SMR; Q89A47; -.
DR   STRING; 224915.bbp_498; -.
DR   PRIDE; Q89A47; -.
DR   EnsemblBacteria; AAO27203; AAO27203; bbp_498.
DR   KEGG; bab:bbp_498; -.
DR   eggNOG; COG0635; Bacteria.
DR   HOGENOM; CLU_027579_2_1_6; -.
DR   OMA; HIPWCVR; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR004559; HemW-like.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR13932; PTHR13932; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00539; hemN_rel; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..374
FT                   /note="Putative heme chaperone HemW-like protein"
FT                   /id="PRO_0000109960"
FT   DOMAIN          1..231
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
SQ   SEQUENCE   374 AA;  44752 MW;  9D93C81AD2565053 CRC64;
     MKLLGLYINI PWPTKRYKYH DFKFPEYKKK INEKKYIHHL LQDLKKDSLL VPNRTINTIF
     IGGIAPNFFK LTSIKYLLKK IKNIIPISKN AENTIEFHIS KLSEKKIFYY KKFGINRFSI
     RIQTFDQKKF NSLSKVHISK NILHKIKKIN IEKFKNINLD LIYGLPKQSL QEALLDLKTA
     ISLKPNHISW CEFYIEKNNN NYKNLSKSCN LNIIWKIFLQ GEKLLKKSGY KKYEISSYSK
     TNYQCLHNLN YWKFGDYLGI GCNAHGKITQ KNGKIIKTIK NKNLKKFMNG KYTYKNHIIS
     KKNLSLEFFM NRLRLNTPIY RKDFKKYTYI SEFYIKNEIK QAIEQNYLIE TKKYWKMTSK
     GIQFLDSLLE IFIT