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Database: UniProt
Entry: A0A0R1Q4M1_9LACO
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ID   A0A0R1Q4M1_9LACO        Unreviewed;       381 AA.
AC   A0A0R1Q4M1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN   ORFNames=FD01_GL002736 {ECO:0000313|EMBL:KRL37780.1};
OS   Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL37780.1, ECO:0000313|Proteomes:UP000051790};
RN   [1] {ECO:0000313|EMBL:KRL37780.1, ECO:0000313|Proteomes:UP000051790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL37780.1,
RC   ECO:0000313|Proteomes:UP000051790};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|RuleBase:RU364116}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364116}.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC       family. HemW subfamily. {ECO:0000256|ARBA:ARBA00006100}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRL37780.1}.
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DR   EMBL; AZEU01000313; KRL37780.1; -; Genomic_DNA.
DR   RefSeq; WP_056965093.1; NZ_AZEU01000313.1.
DR   AlphaFoldDB; A0A0R1Q4M1; -.
DR   PATRIC; fig|1423769.4.peg.2954; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000051790; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR004559; HemW-like.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   NCBIfam; TIGR00539; hemN_rel; 1.
DR   PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR   PANTHER; PTHR13932:SF5; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR   SFLD; SFLDF00288; HemN-like__clustered_with_nucl; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU364116};
KW   Chaperone {ECO:0000256|RuleBase:RU364116};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW   Heme {ECO:0000256|RuleBase:RU364116}; Iron {ECO:0000256|RuleBase:RU364116};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU364116};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051790};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..231
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   381 AA;  44017 MW;  468523BC303E22F1 CRC64;
     MAGAYIHIPF CEHICYYCDF NKVFIEGQPV DDYVAMLLRE MQLVMPQYPN EPIETVYVGG
     GTPTTLTPKQ LDQLCKGIRE ILHFEHGEFT FEANPNDLQA TEKLQVLHDN GVNRLSIGVQ
     SLDDDILKRI GRIHRVKDVY TAIDNARKVG FENLSIDLIF RLPGQSRDNF LHSLRETLAL
     QLPHYSTYSL ILERKTIFYN LMRKGKLTLP SQDIEADMYQ DAIDLMHANG REQYEIANFA
     KPGFECQHNL LYWQNAHYFG FGAGAFGYLG RDRYHNFGPI QQYLAPLHDH KLPVIEHHLV
     PLEEQIEEEM FLGLRTRAGV SRQRFADKFH LQIQDVYGEL LDDLRQQGLV ELNGDQVRLS
     NQGMFLGNEV FQQFLLDDPL V
//
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