HEMW_LACLA
ID HEMW_LACLA Reviewed; 379 AA.
AC Q9CGF7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Heme chaperone HemW;
GN Name=hemW {ECO:0000303|PubMed:22142238}; Synonyms=hemN;
GN OrderedLocusNames=LL1139; ORFNames=L0193;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP FUNCTION, 4FE-4S CLUSTER-BINDING, SUBCELLULAR LOCATION, SUBUNIT, AND
RP HEME-BINDING.
RC STRAIN=IL1403;
RX PubMed=22142238; DOI=10.1042/bj20111618;
RA Abicht H.K., Martinez J., Layer G., Jahn D., Solioz M.;
RT "Lactococcus lactis HemW (HemN) is a haem-binding protein with a putative
RT role in haem trafficking.";
RL Biochem. J. 442:335-343(2012).
CC -!- FUNCTION: Could serve in the delivery of heme to a membrane-localized
CC target protein (Probable). Binds one molecule of heme per monomer,
CC possibly covalently; heme and Fe-S cluster binding are independent.
CC Incubation with the reductant sodium dithionite increases binding. Does
CC not have coproporphyrinogen III dehydrogenase activity in vitro, does
CC not complement an E.coli hemN deletion in vivo (PubMed:22142238). Binds
CC 1 Fe-S cluster, it is probably [4Fe-4S]. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine; only
CC dimeric protein has the cluster (Probable).
CC {ECO:0000269|PubMed:22142238, ECO:0000305|PubMed:22142238}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22142238}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22142238}. Cell
CC membrane {ECO:0000305|PubMed:22142238}. Note=A minor, heme-containing
CC fraction is associated with the cell membrane.
CC {ECO:0000305|PubMed:22142238}.
CC -!- MISCELLANEOUS: L.lactis does not synthesize heme, but is able to take
CC it up from growth medium and to incorporate it into cytochromes.
CC {ECO:0000305}.
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}.
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DR EMBL; AE005176; AAK05237.1; -; Genomic_DNA.
DR PIR; C86767; C86767.
DR RefSeq; NP_267295.1; NC_002662.1.
DR RefSeq; WP_003132086.1; NC_002662.1.
DR AlphaFoldDB; Q9CGF7; -.
DR SMR; Q9CGF7; -.
DR STRING; 272623.L0193; -.
DR PaxDb; Q9CGF7; -.
DR EnsemblBacteria; AAK05237; AAK05237; L0193.
DR KEGG; lla:L0193; -.
DR PATRIC; fig|272623.7.peg.1217; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_2_2_9; -.
DR OMA; HIPWCVR; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA: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; IDA: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; Cell membrane; Chaperone; Cytoplasm; Heme; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..379
FT /note="Heme chaperone HemW"
FT /id="PRO_0000428713"
FT DOMAIN 1..232
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 9
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
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 19
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 22
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 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 379 AA; 43553 MW; 44F295AD2C29D4FD CRC64;
MLQKPNSAYF HIPFCSHICY YCDFAKVLMT GQPIDAYIES LIEEFQSFEI EKLRTIYIGG
GTPSVLSAQQ LERLLTAIAE QLDLEVLEEF TVEANPGDLS DEVIKVLADS AVNRISLGVQ
TFNNALLKKI GRTHTEVQVY DSVERLKKAG FENITIDLIY ALPGQTMEMV KSDVEKFLEL
KLPHVALYSL ILEDHTVFMN RQRRGLLRLP SEDKNADMYE YIMDILAKNG YNHYEVSNFG
LPGFESKHNI TYWDNEEYYG IGAGASGYLA GIRYKNLGPV HHYLKAAPTE KRINEEVLSK
KSQIEEEMFL GLRKKSGVLV EKFENKFKCS FEKLYGEQIT ELINQKLLYN DRQRIHMTDK
GFELGNNVFE KFLLDDINF
