MURJ_BDEBA
ID MURJ_BDEBA Reviewed; 523 AA.
AC Q8VNZ2;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000255|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000255|HAMAP-Rule:MF_02078}; Synonyms=mviN;
GN OrderedLocusNames=Bd1468;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43826 / 109J;
RA Lambert C.;
RT "A novel assay monitering infection of luminescent E. coli by Bdellovibrio
RT bacteriovorus 109J reveals a role for methyl accepting chemotaxis proteins
RT in predation.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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:0000255|HAMAP-Rule:MF_02078}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD12355.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ420185; CAD12355.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX842649; CAE79354.1; -; Genomic_DNA.
DR RefSeq; WP_011163956.1; NC_005363.1.
DR AlphaFoldDB; Q8VNZ2; -.
DR SMR; Q8VNZ2; -.
DR STRING; 264462.Bd1468; -.
DR EnsemblBacteria; CAE79354; CAE79354; Bd1468.
DR KEGG; bba:Bd1468; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_3_7; -.
DR OMA; IFFVAFK; -.
DR OrthoDB; 749401at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008080; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd13123; MATE_MurJ_like; 1.
DR HAMAP; MF_02078; MurJ_MviN; 1.
DR InterPro; IPR004268; MurJ.
DR Pfam; PF03023; MurJ; 1.
DR PIRSF; PIRSF002869; MviN; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
DR TIGRFAMs; TIGR01695; murJ_mviN; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..523
FT /note="Probable lipid II flippase MurJ"
FT /id="PRO_0000181998"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT CONFLICT 90
FT /note="D -> A (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="F -> I (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="V -> L (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..310
FT /note="NR -> SQ (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="V -> A (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="V -> A (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="L -> F (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="K -> R (in Ref. 1; CAD12355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 57434 MW; 2FA2C7BFE221BE3D CRC64;
MSHEASGLKE DRKKVLKSAF LMASGTLTSR ILGLFRDIAL GALFDRAVTD AWTAAFRIPN
LFRRLFGEGS LAVSFIPVFM QTQSEDPTGD RARNLANAFY SLLLVFLGVL TLLGIVYVEP
LFRLILSSDY ALDAAKWELT LRMGRIMFGF VFFVCTYAFY MGILNALGSF GLPALAPALL
NVSMLVFTFM PPQWFAVHGD GLAWGVLIGG LLQALLLAVA LKQRNYLPRL QKTLWTPEVK
AVVRGMLPGL IGMGLLQFST LVNLYFASSL PEGSISYIYW ADRLLELPLS LISVSIGAAL
LPTLSDFANR GLKEKFQETA EESFLMNLFL AWPAALGLYI LAEPIIEVLF LRGKFTVQDV
QMTAAILRIY AVSLLLVSCS RVLMPLYYSV KNTKVPMVLA LVSLAVHVSL APVLMRQWGL
EGLMISGVVA ALINAVLLMG LLKKYSPGIR MSVLLRPALK FVLAGAGMVI SLQAYELLMA
QTGRGLQMLA LFVTILLAVV AYFGLAYVLG CEQISRIRRS SQP
