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Database: UniProt
Entry: A0A063Y641_9GAMM
LinkDB: A0A063Y641_9GAMM
Original site: A0A063Y641_9GAMM 
ID   A0A063Y641_9GAMM        Unreviewed;       302 AA.
AC   A0A063Y641;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   ORFNames=ADINL_1202 {ECO:0000313|EMBL:KDE40610.1};
OS   Nitrincola lacisaponensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE40610.1, ECO:0000313|Proteomes:UP000027318};
RN   [1] {ECO:0000313|EMBL:KDE40610.1, ECO:0000313|Proteomes:UP000027318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4CA {ECO:0000313|EMBL:KDE40610.1,
RC   ECO:0000313|Proteomes:UP000027318};
RX   PubMed=16280482; DOI=10.1099/ijs.0.63647-0;
RA   Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A.,
RA   Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.;
RT   "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic
RT   bacterium isolated from an alkaline, saline lake.";
RL   Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005).
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:KDE40610.1}.
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DR   EMBL; JMSZ01000016; KDE40610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A063Y641; -.
DR   STRING; 267850.ADINL_1202; -.
DR   PATRIC; fig|267850.7.peg.1197; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000027318; 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:KDE40610.1};
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:KDE40610.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027318};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         181
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         194
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         198
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ   SEQUENCE   302 AA;  34136 MW;  A5A1941DC0425693 CRC64;
     MQLSLGPLLY YWPAEQVDAF YQQAAEWPVE VVHLGETVCS RRRELKLDDW ERIGKHLVAS
     GKQVVLSTQA LIESEADLKQ LRRLLDLAAE QGWQVEANDQ SALYYLTEAE LPFTTGPSLN
     IYNLRTLSNL SALGLQRWCL PVELSRETLA DLQQGIAEQQ LDLETEVFAY GHLPLAWSSR
     CFTARYHDLP KDRCGFVCQQ YAAGLPMRTQ ESRDVFVLNG IQTLSGACCN LLDQLPLMRR
     HGVQVVRLSP QAEGMAAVVS QFDRMRSGEL PLGQEIPLHA QQDCNGYWFG RPGMDRVNPL
     MD
//
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