GenomeNet

Database: UniProt
Entry: A0A1B1MGL9_STRLN
LinkDB: A0A1B1MGL9_STRLN
Original site: A0A1B1MGL9_STRLN 
ID   A0A1B1MGL9_STRLN        Unreviewed;       371 AA.
AC   A0A1B1MGL9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=SLCG_2881 {ECO:0000313|EMBL:AXG54036.1}, SLINC_5534
GN   {ECO:0000313|EMBL:ANS67758.1};
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS67758.1, ECO:0000313|Proteomes:UP000092598};
RN   [1] {ECO:0000313|EMBL:ANS67758.1, ECO:0000313|Proteomes:UP000092598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS67758.1,
RC   ECO:0000313|Proteomes:UP000092598};
RA   Meng S.C.;
RT   "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT   actinobacteria.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AXG54036.1, ECO:0000313|Proteomes:UP000253884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC-G {ECO:0000313|EMBL:AXG54036.1,
RC   ECO:0000313|Proteomes:UP000253884};
RX   PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA   Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA   Wu H., Bai L., Zhang L., Zhang B.;
RT   "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT   Streptomyces lincolnensis.";
RL   J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC       apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP-Rule:MF_02040}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02040}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       {ECO:0000256|HAMAP-Rule:MF_02040}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the Mrp/NBP35 ATP-
CC       binding proteins family. {ECO:0000256|ARBA:ARBA00008205}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MIP18 family.
CC       {ECO:0000256|ARBA:ARBA00007352}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP016438; ANS67758.1; -; Genomic_DNA.
DR   EMBL; CP022744; AXG54036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B1MGL9; -.
DR   STRING; 1915.SLINC_5534; -.
DR   KEGG; sls:SLINC_5534; -.
DR   PATRIC; fig|1915.4.peg.6135; -.
DR   Proteomes; UP000092598; Chromosome.
DR   Proteomes; UP000253884; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd02037; Mrp_NBP35; 1.
DR   Gene3D; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR002744; MIP18-like.
DR   InterPro; IPR000808; Mrp-like_CS.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR044304; NUBPL-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR42961; IRON-SULFUR PROTEIN NUBPL; 1.
DR   PANTHER; PTHR42961:SF2; IRON-SULFUR PROTEIN NUBPL; 1.
DR   Pfam; PF01883; FeS_assembly_P; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02040}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02040};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02040}; Reference proteome {ECO:0000313|Proteomes:UP000092598}.
FT   DOMAIN          2..70
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         113..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   371 AA;  38313 MW;  446B8FE3AA49CB76 CRC64;
     MREALSTVND PEINRPITEL GMVKSVEIGA DGAVAVTVYL TVSGCPMRDT ITQRVTDAVS
     AVEGVTRVDV TLDVMSDEQR KELATALRGG QTEREVPFAK PGSLTRVYAV ASGKGGVGKS
     SVTVNLAAAM AADGLKVGVV DADIYGHSVP RMLGADGTPT QVENMIMPPS AHGVKVISIG
     MFTPGNSAVV WRGPMLHRAL QQFLSDVYWG DLDVLLLDLP PGTGDIAISV AQLVPNAEIL
     VVTTPQQAAA EVAERAGSIA VQTHQKIVGV VENMAGLPCP HCGEMVDVFG TGGGQSVADG
     LTRTTGASVP VLGSIPIDVR LREGGDDGRP VVLTDPDSPA GSALRAIAGK LGGRQRGLSG
     LSLGITPKNK F
//
DBGET integrated database retrieval system