HEMW_ECOLI
ID HEMW_ECOLI Reviewed; 378 AA.
AC P52062; Q2M9N8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Heme chaperone HemW {ECO:0000303|PubMed:29282292};
GN Name=hemW {ECO:0000303|PubMed:29282292}; Synonyms=yggW;
GN OrderedLocusNames=b2955, JW2922;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FE-S CLUSTER.
RC STRAIN=K12;
RA Hauert J.;
RL Thesis (1977), University of Geneva, Switzerland.
RN [4]
RP FUNCTION, 4FE-4S CLUSTER, SUBUNIT, DISRUPTION PHENOTYPE, HEME-BINDING, AND
RP MUTAGENESIS OF 16-CYS--CYS-23.
RX PubMed=29282292; DOI=10.1074/jbc.ra117.000229;
RA Haskamp V., Karrie S., Mingers T., Barthels S., Alberge F., Magalon A.,
RA Mueller K., Bill E., Lubitz W., Kleeberg K., Schweyen P., Broering M.,
RA Jahn M., Jahn D.;
RT "The radical SAM protein HemW is a heme chaperone.";
RL J. Biol. Chem. 293:2558-2572(2018).
CC -!- FUNCTION: Probably acts as a heme chaperone, transferring heme to the
CC NarI subunit of the respiratory enzyme nitrate reductase; transfer may
CC be stimulated by NADH. Binds one molecule of heme per monomer, possibly
CC covalently. Heme binding is not affected by either [4Fe-4S] or S-
CC adenosyl-L-methionine (SAM)-binding. Does not have coproporphyrinogen
CC III dehydrogenase activity in vitro (PubMed:29282292). Binds 1 [4Fe-4S]
CC cluster. The cluster is coordinated with 3 cysteines and an
CC exchangeable S-adenosyl-L-methionine (Probable).
CC {ECO:0000269|PubMed:29282292, ECO:0000305|PubMed:29282292}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- SUBUNIT: Binding of the [4Fe-4S] cofactor promotes dimerization.
CC {ECO:0000269|PubMed:29282292}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:29282292}.
CC -!- DISRUPTION PHENOTYPE: Very slightly decreased anaerobic growth in
CC minimal medium with KNO(3) and glycerol. {ECO:0000269|PubMed:29282292}.
CC -!- MISCELLANEOUS: Might carry two S-adenosyl-L-methionine binding sites
CC with only one binding to the iron-sulfur cluster.
CC {ECO:0000305|PubMed:29282292}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000305}.
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DR EMBL; U28377; AAA69122.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75992.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77018.1; -; Genomic_DNA.
DR PIR; B65081; B65081.
DR RefSeq; NP_417430.1; NC_000913.3.
DR RefSeq; WP_000239943.1; NZ_SSUV01000019.1.
DR AlphaFoldDB; P52062; -.
DR SMR; P52062; -.
DR BioGRID; 4262352; 41.
DR BioGRID; 851766; 5.
DR IntAct; P52062; 15.
DR STRING; 511145.b2955; -.
DR jPOST; P52062; -.
DR PaxDb; P52062; -.
DR PRIDE; P52062; -.
DR EnsemblBacteria; AAC75992; AAC75992; b2955.
DR EnsemblBacteria; BAE77018; BAE77018; BAE77018.
DR GeneID; 947446; -.
DR KEGG; ecj:JW2922; -.
DR KEGG; eco:b2955; -.
DR PATRIC; fig|1411691.4.peg.3777; -.
DR EchoBASE; EB2808; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_2_1_6; -.
DR InParanoid; P52062; -.
DR OMA; HIPWCVR; -.
DR PhylomeDB; P52062; -.
DR BioCyc; EcoCyc:G7531-MON; -.
DR PRO; PR:P52062; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISS: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 1: Evidence at protein level;
KW 4Fe-4S; Chaperone; Cytoplasm; Heme; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..378
FT /note="Heme chaperone HemW"
FT /id="PRO_0000109956"
FT DOMAIN 1..237
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 10
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 16
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 20
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 23
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 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 67..68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT MUTAGEN 16..23
FT /note="CVQKCPYC->SVQKSPYS: Loss of [4Fe-4S] cofactor,
FT protein does not dimerize, binds heme, does not transfer
FT heme to NarGHI."
FT /evidence="ECO:0000269|PubMed:29282292"
SQ SEQUENCE 378 AA; 42584 MW; 00A115BFDE4386AF CRC64;
MVKLPPLSLY IHIPWCVQKC PYCDFNSHAL KGEVPHDDYV QHLLNDLDND VAYAQGREVK
TIFIGGGTPS LLSGPAMQTL LDGVRARLPL AADAEITMEA NPGTVEADRF VDYQRAGVNR
ISIGVQSFSE EKLKRLGRIH GPQEAKRAAK LASGLGLRSF NLDLMHGLPD QSLEEALGDL
RQAIELNPPH LSWYQLTIEP NTLFGSRPPV LPDDDALWDI FEQGHQLLTA AGYQQYETSA
YAKPGYQCQH NLNYWRFGDY IGIGCGAHGK VTFPDGRILR TTKTRHPRGF MQGRYLESQR
DVEATDKPFE FFMNRFRLLE AAPRVEFIAY TGLCEDVIRP QLDEAIAQGY LTECADYWQI
TEHGKLFLNS LLELFLAE
