ID A0A1V3RRL9_9BURK Unreviewed; 521 AA.
AC A0A1V3RRL9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN ORFNames=B0E41_24880 {ECO:0000313|EMBL:OOG79073.1};
OS Hydrogenophaga sp. A37.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG79073.1, ECO:0000313|Proteomes:UP000189189};
RN [1] {ECO:0000313|EMBL:OOG79073.1, ECO:0000313|Proteomes:UP000189189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A37 {ECO:0000313|EMBL:OOG79073.1,
RC ECO:0000313|Proteomes:UP000189189};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid-
CC linked peptidoglycan precursors from the inner to the outer leaflet of
CC the cytoplasmic membrane. {ECO:0000256|HAMAP-Rule:MF_02078,
CC ECO:0000256|PIRNR:PIRNR002869}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02078}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000256|HAMAP-
CC Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
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:OOG79073.1}.
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DR EMBL; MUNZ01000188; OOG79073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3RRL9; -.
DR STRING; 1945864.B0E41_24880; -.
DR OrthoDB; 9816572at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000189189; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd13123; MATE_MurJ_like; 1.
DR HAMAP; MF_02078; MurJ_MviN; 1.
DR InterPro; IPR004268; MurJ.
DR NCBIfam; TIGR01695; murJ_mviN; 1.
DR PANTHER; PTHR47019; LIPID II FLIPPASE MURJ; 1.
DR PANTHER; PTHR47019:SF1; LIPID II FLIPPASE MURJ; 1.
DR Pfam; PF03023; MurJ; 1.
DR PIRSF; PIRSF002869; MviN; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02078};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02078};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02078}; Reference proteome {ECO:0000313|Proteomes:UP000189189};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transport {ECO:0000256|HAMAP-Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
FT TRANSMEM 90..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 134..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 190..219
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 281..299
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 394..413
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 419..440
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 492..513
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 521 AA; 55546 MW; 84AC768E9A201C21 CRC64;
MSLFKSASLV SLLTLASRIT GLVRQLLLAS MFGASPLTDA FNVAFRIPNM FRRLFAEGAF
SQAFVPVLAG ARATQGDEAT RELVDQIATV LVWALLVTCV LGVAASPILV WAMASGLKQS
AQGFEAAVFM TRWMFPYIGF MSLVALSAGV LNTWKRFAVP AATPVLLNVA MIGAAWLGAP
WFKTLGIEPI YAMAGGVMLG GMLQLGVQIP ALLRIGMLPR VGLRWSSLKK AWTHPGTRRV
TTLMLPALLG VSVAQISLLI NTQIASHLTP GSVSWLSYAD LLMEFPTAML GVALGVVLLP
QLSAAKAQED GARYSQLLDW GLRLMVLLAV PCALALLTFA KPLVSGLYHY GAFTERDVQQ
TSLALMGYGA GLLGLVAIKV LAPGFYARQD IRTPALIAVL VLVLTQGMNL LFVPHLAHAG
LALSIGLGAA LNALLLLIGL RRRGAYQPLP GWGRFALQVV AASALMAVFL LWAAGAENWT
DFEGRALERV GLLALCVVGA AAIYFVALLL SGLKLRQFVR K
//
