ID C9MRA3_9BACT Unreviewed; 286 AA.
AC C9MRA3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ORFNames=HMPREF0973_02139 {ECO:0000313|EMBL:EEX18076.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX18076.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX18076.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX18076.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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: 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:EEX18076.1}.
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DR EMBL; ACVA01000048; EEX18076.1; -; Genomic_DNA.
DR RefSeq; WP_004383837.1; NZ_GG698715.1.
DR AlphaFoldDB; C9MRA3; -.
DR STRING; 649761.HMPREF0973_02139; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_2_0_10; -.
DR OrthoDB; 9808289at2; -.
DR Proteomes; UP000003327; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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 HAMAP; MF_01006; Undec_diphosphatase; 1.
DR InterPro; IPR003824; UppP.
DR PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR PANTHER; PTHR30622:SF3; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR Pfam; PF02673; BacA; 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:UP000003327};
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 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
FT TRANSMEM 262..285
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01006"
SQ SEQUENCE 286 AA; 31881 MW; E0E17C35EB0FB371 CRC64;
MTLIQTIIIS IVEGLTEFLP VSSTGHMIIT QHLLGVSQGS PFVHAFTFII QFGAILSVVC
LYWKRFFHID RTPVPADVEN PFLRFIHPLR FYWLLFVGVL PAVVIGLAAK KSGLLDWLLD
SIWAVAIMLV VGGIFMLFCD KIFNKGREEN KVNEKRAFNI GLWQCLSVIP GTSRSMATIV
GGMANGLTRK RAAEYSFFLA VPTMAGATLL DLLDILKEDA TWVNTHDLIM LAVGCVVSFV
VALLAMKWFV SFLTKYGFKV FGWYRIIIGI IIIVMLLSGI SLNMVD
//