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Database: UniProt
Entry: E6SKB0_THEM7
LinkDB: E6SKB0_THEM7
Original site: E6SKB0_THEM7 
ID   E6SKB0_THEM7            Unreviewed;       431 AA.
AC   E6SKB0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   OrderedLocusNames=Tmar_2188 {ECO:0000313|EMBL:ADU52268.1};
OS   Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS   7p75a).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX   NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU52268.1, ECO:0000313|Proteomes:UP000008915};
RN   [1] {ECO:0000313|EMBL:ADU52268.1, ECO:0000313|Proteomes:UP000008915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC   {ECO:0000313|Proteomes:UP000008915};
RX   PubMed=21304738;
RA   Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA   Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Thermaerobacter marianensis type strain
RT   (7p75a).";
RL   Stand. Genomic Sci. 3:337-345(2010).
RN   [2] {ECO:0000313|Proteomes:UP000008915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC   {ECO:0000313|Proteomes:UP000008915};
RX   DOI=10.4056/sigs.1373474;
RA   Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA   Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT   "Complete genome sequence of Thermaerobacter marianensis type strain
RT   (7p75aT).";
RL   Stand. Genomic Sci. 3:337-345(2010).
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}.
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DR   EMBL; CP002344; ADU52268.1; -; Genomic_DNA.
DR   RefSeq; WP_013496568.1; NC_014831.1.
DR   AlphaFoldDB; E6SKB0; -.
DR   STRING; 644966.Tmar_2188; -.
DR   KEGG; tmr:Tmar_2188; -.
DR   eggNOG; COG0635; Bacteria.
DR   HOGENOM; CLU_027579_2_0_9; -.
DR   Proteomes; UP000008915; Chromosome.
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; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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   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|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364116};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU364116};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364116};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364116};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008915};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          47..281
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  47371 MW;  8E5941BB63AC9AD6 CRC64;
     MKAPRAEART GLGAGTNAAP AGPAARKAGG RPDGSTRDAC GPAASWPEWD AGPALYVHVP
     YCRQRCYYCD FNTYLLDPEG KARYLAALQR ELALLATDPG LTRPLVSVYV GGGTPSILEP
     AELERLLGAV HRHFCLAPDA EITVECNPGT LDEGRLAALR DGGVTRLSLG LQAVQDELLR
     AMGRDHTWAD FCATYRRVRQ AGFDNVNIDL IFGLPGQTLD QWEASLRAVV DLDPEHVSCY
     GLELHPGTPF HRWWEAGELV LPGEDAERAM FDLAYERLGA AGFVRYEISN FARPGRESVH
     NRVYWLNGSY LGAGPGAWSC WRGERRRNRL HPAAYAAELA EDRLPVDVRE PVDRRRAMEE
     TMILGLRLAE GVDEARFARR FGLTPAEAFP AAVARLLDEG WLVREGGRLR LSPGAVPVAN
     SVLAYFVEPE E
//
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