ID   MURJ_AQUAE              Reviewed;         499 AA.
AC   O67658;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=aq_1789;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}.
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DR   EMBL; AE000657; AAC07622.1; -; Genomic_DNA.
DR   PIR; H70453; H70453.
DR   RefSeq; NP_214224.1; NC_000918.1.
DR   RefSeq; WP_010881161.1; NC_000918.1.
DR   AlphaFoldDB; O67658; -.
DR   SMR; O67658; -.
DR   STRING; 224324.aq_1789; -.
DR   EnsemblBacteria; AAC07622; AAC07622; aq_1789.
DR   KEGG; aae:aq_1789; -.
DR   PATRIC; fig|224324.8.peg.1381; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_006797_5_0_0; -.
DR   InParanoid; O67658; -.
DR   OMA; IFFVAFK; -.
DR   OrthoDB; 749401at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0034204; P:lipid translocation; IBA:GO_Central.
DR   GO; GO:0015836; P:lipid-linked peptidoglycan transport; IBA:GO_Central.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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..499
FT                   /note="Probable lipid II flippase MurJ"
FT                   /id="PRO_0000181997"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   499 AA;  56435 MW;  31E9B69124FB0903 CRC64;
     MPSLFRASLL FSLGILLSRI FGYVRDATVA YYFGASAVSD AFFIAFRIPN AFRRIFGEGG
     FNAVFIPFYG EAVKQNREEE FLRKTFGLLI TFSLSVVIIG LLFPEEIISV ISPGIKEKET
     FSYAVEFLKF TILYLPLVSF YAYSMAILLV QGKFFVPSVS QTLFNLGFIL SLVILFHTLG
     HYSLALAVLI GGLFQIIPNT FLLFKEKLLK IPKFSLDREI KTFLKKFLFT LGGFSANQLS
     LFVDTFLASF LKVGSISYVY YAARIYLLPI SLFSISLSNT LLALVSTKKD KEKDTDTALK
     LTLMLSIPSS FGLFFLSREI VSVLYKRGNF SEEDLFYTSG LLSLYAFSVP FYSLQHILKT
     VYYSKKNVEI PTKSAFLSVF LEALFGSVFI FLLNFGVYSF PLAALISSSS VLVYLYQKLP
     QKVSIPFGNL IKYLIASSFM GGLVYLTESL TQNPFILVSF IPIYALFYYV FLIILREELA
     ILISYGIFRR GKILQRESN