ID   MURJ_BUCBP              Reviewed;         513 AA.
AC   Q89AI1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=bbp_309;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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   ---------------------------------------------------------------------------
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; AE016826; AAO27031.1; -; Genomic_DNA.
DR   RefSeq; WP_011091432.1; NC_004545.1.
DR   AlphaFoldDB; Q89AI1; -.
DR   SMR; Q89AI1; -.
DR   STRING; 224915.bbp_309; -.
DR   EnsemblBacteria; AAO27031; AAO27031; bbp_309.
DR   GeneID; 56470848; -.
DR   KEGG; bab:bbp_309; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_006797_5_3_6; -.
DR   OMA; IFFVAFK; -.
DR   OrthoDB; 749401at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000601; 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..513
FT                   /note="Probable lipid II flippase MurJ"
FT                   /id="PRO_0000182002"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   513 AA;  58590 MW;  493DE50969EDB088 CRC64;
     MNILKSLISL SLITFISRIL GFMRDLLIAY SFGASGITDA FFLAFKIPNL FRRIFAEGAF
     SQVFIPILSE YKNNKNIELT RNFISNILGL MIIILSLFTA FGIYFANDIV KICAPGFINS
     HEKLYLATKM LKIMFPYIFF VSLGSLTGSI LNAWNYFSVP AYSSIFLNLS MIMFISFVTA
     YFNPKILSLA WAVIVGGVFQ ILYQFPYLKN INMLIFPKFN ILNLGVLKFL KQIGIVALGM
     SVNQVSIIIA TISSSFLISG SISWIYYSDR LVEFISGIFG VSLSTILLPL LSKSVNNINI
     KEYSRLLNWA LRLVCILVIP SIIILFTLSE SLITLLFKYG AFTYNDVIMT KNVIEFYSIG
     LLPFVLIKIL LAGFYSIRNV KTPMKISIFI LVLTQLMNIF FIKYFQYTSF ALAISLASWI
     NFFLLYRKLC QSEFFIPSTN WLRFLLKIFA AAMVMLILLF INKNLILSAN THSIFFKILR
     LFYICASSGG GYLFTLFCLG LRFNHFYLKS YKY