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Database: UniProt
Entry: A0A011MF98_9PROT
LinkDB: A0A011MF98_9PROT
Original site: A0A011MF98_9PROT 
ID   A0A011MF98_9PROT        Unreviewed;       307 AA.
AC   A0A011MF98;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   ORFNames=AW08_01240 {ECO:0000313|EMBL:EXI68458.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI68458.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI68458.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for O(2)-independent ubiquinone (coenzyme Q)
CC       biosynthesis. Together with UbiU, is essential for the C6-hydroxylation
CC       reaction in the oxygen-independent ubiquinone biosynthesis pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02233}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02233};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02233}.
CC   -!- SUBUNIT: Forms an heterodimer with UbiU. {ECO:0000256|HAMAP-
CC       Rule:MF_02233}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. UbiV subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02233}.
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:EXI68458.1}.
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DR   EMBL; JFAX01000005; EXI68458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011MF98; -.
DR   STRING; 1454001.AW08_01240; -.
DR   PATRIC; fig|1454001.3.peg.1264; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000020218; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02233; UbiV; 1.
DR   InterPro; IPR001539; Peptidase_U32.
DR   InterPro; IPR043693; UbiV.
DR   PANTHER; PTHR30217; PEPTIDASE U32 FAMILY; 1.
DR   PANTHER; PTHR30217:SF11; UBIQUINONE BIOSYNTHESIS PROTEIN UBIV; 1.
DR   Pfam; PF01136; Peptidase_U32; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Hydrolase {ECO:0000313|EMBL:EXI68458.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02233};
KW   Protease {ECO:0000313|EMBL:EXI68458.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT   BINDING         40
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         178
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         191
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         195
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ   SEQUENCE   307 AA;  33391 MW;  DDD077125E3A2D16 CRC64;
     MKLSLGPLLY FWPKHEVFEF YAEMAQQPAL DIICLGEVVC SRRQQMRSAD WLGLARDLAA
     AGKEVVIAAQ ALLESESDLK ALRRLADEAS EIPGCLLEAN DLGAVGIAAG RPFVAGPHLN
     IYNEATLASF ARRGMRRWLP PLEADRRLIE TLHGTRPAGV ATEVFVFGKL PLAFSARCFT
     ARHYNLGKDD CQFRCLDHPQ GMTLRTREGQ PFLSINGIQT MSAQTCSLLP QVPDLLAMGI
     EVIRISPQPQ AMTAVIAAFD AARRGAAVAP DTSGWASDGL VDGYWFGDAG IACHQAATRV
     NREGIQS
//
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