ID A0A1Q2MBA6_9BACT Unreviewed; 455 AA.
AC A0A1Q2MBA6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|ARBA:ARBA00021581, ECO:0000256|HAMAP-Rule:MF_01006};
DE EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374, ECO:0000256|HAMAP-Rule:MF_01006};
DE AltName: Full=Bacitracin resistance protein {ECO:0000256|ARBA:ARBA00032932, ECO:0000256|HAMAP-Rule:MF_01006};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707, ECO:0000256|HAMAP-Rule:MF_01006};
GN Name=uppP {ECO:0000256|HAMAP-Rule:MF_01006,
GN ECO:0000313|EMBL:AQQ69949.1};
GN ORFNames=SMSP2_00283 {ECO:0000313|EMBL:AQQ69949.1};
OS Limihaloglobus sulfuriphilus.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Sedimentisphaeraceae; Limihaloglobus.
OX NCBI_TaxID=1851148 {ECO:0000313|EMBL:AQQ69949.1, ECO:0000313|Proteomes:UP000188181};
RN [1] {ECO:0000313|Proteomes:UP000188181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-Chi-D1 {ECO:0000313|Proteomes:UP000188181};
RA Spring S., Bunk B., Sproer C.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC (UPP). Confers resistance to bacitracin. {ECO:0000256|HAMAP-
CC Rule:MF_01006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC Evidence={ECO:0000256|ARBA:ARBA00000759, ECO:0000256|HAMAP-
CC Rule:MF_01006};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01006};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01006}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- MISCELLANEOUS: Bacitracin is thought to be involved in the inhibition
CC of peptidoglycan synthesis by sequestering undecaprenyl diphosphate,
CC thereby reducing the pool of lipid carrier available.
CC {ECO:0000256|HAMAP-Rule:MF_01006}.
CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|ARBA:ARBA00010621,
CC ECO:0000256|HAMAP-Rule:MF_01006}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01006}.
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; CP019646; AQQ69949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2MBA6; -.
DR STRING; 1851148.SMSP2_00283; -.
DR KEGG; pbas:SMSP2_00283; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000188181; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:InterPro.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR CDD; cd06971; PgpA; 1.
DR HAMAP; MF_01006; Undec_diphosphatase; 1.
DR InterPro; IPR036681; PgpA-like_sf.
DR InterPro; IPR003824; UppP.
DR InterPro; IPR007686; YutG/PgpA.
DR PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR PANTHER; PTHR30622:SF2; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR Pfam; PF02673; BacA; 1.
DR Pfam; PF04608; PgpA; 1.
DR SUPFAM; SSF101307; YutG-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW Rule:MF_01006};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01006}; Cell shape {ECO:0000256|HAMAP-Rule:MF_01006};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01006};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01006};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006};
KW Reference proteome {ECO:0000313|Proteomes:UP000188181};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01006};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01006}.
FT TRANSMEM 29..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 89..115
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 303..320
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 332..351
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 435..452
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT DOMAIN 5..156
FT /note="YutG/PgpA"
FT /evidence="ECO:0000259|Pfam:PF04608"
SQ SEQUENCE 455 AA; 49097 MW; 512D07D047C95801 CRC64;
MKRIFTSCFG LGFMPVASGT WGSLLPVVVF MAMGTFAAPA AAITAVLLLS GIFFSFICVR
YGTQVADEMQ LKDPGEIVAD EYAGQALTLI LAVLFGGYTA GEPVCLMAGA AFLLFRLFDI
VKPWPIRSLE KYPGGWGVLL DDLLAGVYAG VVYIIVAKTG IIERLDCLTC SGSASGGLTV
DMAVVLGIVQ GLTEFLPVSS SGHLVVFEDL FAGLDPDTAE MLLFDLSIHV GTVIAVIAVF
YKDIIKLVTG FFNWKDTGFK PLALYRENDN VHFAAAMIVT IITTFIFYKI FEEPLDSARK
VKVVVVMWLV TAALLFITDL KKDTTKTLRQ IGLFSAAIIG AAQAAAILPG ISRSGATICA
AILLGLKRDK AVEYSFFVAI PVILGASVLE FIDKYDLISG SHISPLIFAA GMAASFLTGI
AALKLLINLS RQRRLKWFSI YLFIVAALVF YFEIM
//
