HEMW_BACSU
ID HEMW_BACSU Reviewed; 379 AA.
AC P54304;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Heme chaperone HemW;
GN Name=hemW {ECO:0000250|UniProtKB:P52062};
GN Synonyms=hemN {ECO:0000303|PubMed:8757728}, yqeR;
GN OrderedLocusNames=BSU25500;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=168;
RX PubMed=8757728; DOI=10.1099/13500872-142-7-1641;
RA Homuth G., Heinemann M., Zuber U., Schumann W.;
RT "The genes of lepA and hemN form a bicistronic operon in Bacillus
RT subtilis.";
RL Microbiology 142:1641-1649(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 94 AND 365-379.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-366.
RC STRAIN=168 / MB11;
RX PubMed=1339421; DOI=10.1128/jb.174.10.3300-3310.1992;
RA Wetzstein M., Voelker U., Dedio J., Loebau S., Zuber U., Schiesswohl M.,
RA Herget C., Hecker M., Schumann W.;
RT "Cloning, sequencing, and molecular analysis of the dnaK locus from
RT Bacillus subtilis.";
RL J. Bacteriol. 174:3300-3310(1992).
RN [6]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9371469; DOI=10.1128/jb.179.22.7181-7185.1997;
RA Hippler B., Homuth G., Hoffmann T., Hungerer C., Schumann W., Jahn D.;
RT "Characterization of Bacillus subtilis hemN.";
RL J. Bacteriol. 179:7181-7185(1997).
RN [7]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10498703; DOI=10.1128/jb.181.19.5922-5929.1999;
RA Homuth G., Rompf A., Schumann W., Jahn D.;
RT "Transcriptional control of Bacillus subtilis hemN and hemZ.";
RL J. Bacteriol. 181:5922-5929(1999).
RN [8]
RP CAUTION.
RC STRAIN=168;
RA Hauert J.;
RL Thesis (1977), University of Geneva, Switzerland.
CC -!- FUNCTION: Probably acts as a heme chaperone, transferring heme to an
CC unknown acceptor. Binds one molecule of heme per monomer, possibly
CC covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is
CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine (By similarity). {ECO:0000250|UniProtKB:P32131,
CC ECO:0000250|UniProtKB:P52062}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CGF7}.
CC -!- INDUCTION: Part of the lepA-hemN operon; there is a strong
CC transcriptional terminator between the 2 genes, this gene is much less
CC transcribed. There can be further readthough downstream
CC (PubMed:8757728, PubMed:9371469). Induced under anaerobic conditions by
CC resDE, fnr and arfM. {ECO:0000269|PubMed:10498703,
CC ECO:0000269|PubMed:8757728, ECO:0000269|PubMed:9371469}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate
CC coproporphyrinogen-III under anaerobic conditions, but show normal
CC growth under aerobic and anaerobic conditions.
CC {ECO:0000269|PubMed:10498703, ECO:0000269|PubMed:9371469}.
CC -!- MISCELLANEOUS: Might carry two S-adenosyl-L-methionine binding sites
CC with only one binding to the iron-sulfur cluster.
CC {ECO:0000250|UniProtKB:P32131}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000305}.
CC -!- CAUTION: Although the bacteria accumulates coproporphyrinogen-III when
CC the gene is disrupted, no oxygen-independent coproporphyrinogen-III
CC oxidase activity or complementation have been shown. The exact role of
CC this protein is unknown. {ECO:0000305|PubMed:10498703,
CC ECO:0000305|PubMed:9371469}.
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DR EMBL; X91655; CAB61616.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12461.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14492.2; -; Genomic_DNA.
DR EMBL; M84964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B69640; B69640.
DR RefSeq; NP_390428.2; NC_000964.3.
DR RefSeq; WP_004398764.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54304; -.
DR SMR; P54304; -.
DR STRING; 224308.BSU25500; -.
DR PaxDb; P54304; -.
DR PRIDE; P54304; -.
DR EnsemblBacteria; CAB14492; CAB14492; BSU_25500.
DR GeneID; 937845; -.
DR KEGG; bsu:BSU25500; -.
DR PATRIC; fig|224308.179.peg.2771; -.
DR eggNOG; COG0635; Bacteria.
DR InParanoid; P54304; -.
DR OMA; HIPWCVR; -.
DR PhylomeDB; P54304; -.
DR BioCyc; BSUB:BSU25500-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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 Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00539; hemN_rel; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Chaperone; Cytoplasm; Heme; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..379
FT /note="Heme chaperone HemW"
FT /id="PRO_0000109939"
FT DOMAIN 1..233
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 5
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 61..62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT CONFLICT 94
FT /note="E -> D (in Ref. 2; BAA12461)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="I -> S (in Ref. 1; CAB61616)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..379
FT /note="KLLGNEVFGAFLGEL -> NY (in Ref. 1; CAB61616, 2;
FT BAA12461 and 5; M84964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42888 MW; ECEC9FC2D638D3FF CRC64;
MKSAYIHIPF CEHICHYCDF NKYFIQSQPV DEYLNALEQE MINTIAKTGQ PDLKTIFIGG
GTPTSLSEEQ LKKLMDMINR VLKPSSDLSE FAVEANPDDL SAEKLKILKE AGVNRLSFGV
QTFEDDLLEK IGRVHKQKDV FTSFERAREI GFENISLDLM FGLPGQTLKH LEHSINTALS
LDAEHYSVYS LIVEPKTVFY NLMQKGRLHL PPQEQEAEMY EIVMSKMEAH GIHQYEISNF
AKAGMESKHN LTYWSNEQYF GFGAGAHGYI GGTRTVNVGP VKHYIDLIAE KGFPYRDTHE
VTTEEQIEEE MFLGLRKTAG VSKKRFAEKY GRSLDGLFPS VLKDLAEKGL IHNSESAVYL
THQGKLLGNE VFGAFLGEL
