ID A0A1X3PBU0_9MICC Unreviewed; 423 AA.
AC A0A1X3PBU0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN ORFNames=BCY76_000910 {ECO:0000313|EMBL:OSM44696.1};
OS Nesterenkonia sp. PF2B19.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=1881858 {ECO:0000313|EMBL:OSM44696.1, ECO:0000313|Proteomes:UP000175621};
RN [1] {ECO:0000313|EMBL:OSM44696.1, ECO:0000313|Proteomes:UP000175621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF2B19 {ECO:0000313|EMBL:OSM44696.1,
RC ECO:0000313|Proteomes:UP000175621};
RX PubMed=28408669;
RA Singh P., Kapse N., Roy U., Singh S.M., Dhakephalkar P.K.;
RT "Draft Genome Sequence of Permafrost Bacterium Nesterenkonia sp. Strain
RT PF2B19, Revealing a Cold Adaptation Strategy and Diverse Biotechnological
RT Potential.";
RL Genome Announc. 5:e00133-17(2017).
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:OSM44696.1}.
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DR EMBL; MDSS02000002; OSM44696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3PBU0; -.
DR STRING; 1881858.BCY76_000910; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000175621; 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; 3.20.20.70; 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; 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; PF04055; Radical_SAM; 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 SFLD; SFLDS00029; Radical_SAM; 2.
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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 25..271
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 423 AA; 45721 MW; 7C7192FF97F7179B CRC64;
MPATLPVGDP VPADGALPAR VLAGLGGRAS APLGLYVHIP FCSVRCGYCD FNTYTAEDLG
PGASRESYPE TLIRELEFAA DLLARSGAPE RPLRTIFFGG GTPTLLPAES LARILERARS
LFGVAPGAEV TTEANPDTVD EATAATLAEA GFTRVSLGMQ SAVPKVLRTL DRTHDPANVT
RAVDAVRSQG LQVSLDLIYG TPGETLEDWR TSLETAVAMD PDHVSAYSLI VEEGTAMAAK
VRRGELPDVD PDDHADKYLL TDELLSAAGH QWYEVSNFSR DESTRSQHNL NYWRDSDWWG
AGPGAHSHLG GLRWWNVKHP AAYAQRLHQG ITPGHGRELL DDDAQALEHL MLRLRIAEGL
DVAEHEALPG ARRLDDGVLR ALVHEGLAQE GPLNPDERSP RGRVVLTLQG RLLADAVTRR
LSG
//
