ID   MURJ_BUCAP              Reviewed;         514 AA.
AC   Q8K9L3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=BUsg_321;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67875.1; -; Genomic_DNA.
DR   RefSeq; WP_011053842.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9L3; -.
DR   SMR; Q8K9L3; -.
DR   STRING; 198804.BUsg_321; -.
DR   EnsemblBacteria; AAM67875; AAM67875; BUsg_321.
DR   KEGG; bas:BUsg_321; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_006797_5_3_6; -.
DR   OMA; IFFVAFK; -.
DR   OrthoDB; 749401at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000416; 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   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..514
FT                   /note="Probable lipid II flippase MurJ"
FT                   /id="PRO_0000182001"
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        92..112
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        157..177
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        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        315..335
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        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT   TRANSMEM        448..468
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   514 AA;  59242 MW;  6E619293FFAF99E9 CRC64;
     MNILKSLISV GIMTLISRIF GFFRDVLIAH IFGASMFTDA FFIAFKIPNL LRRIFAEGAF
     YQSFIPILID YKSRKDKEYI QEFIRSTCGF TILVLTTFVI LGIIFSDYII FISAPGFSES
     SKKLQLASNL LKIMFPYILF ISLSSLCSSI LNSYNYFFIP SLSSSLLNIS IIVFSFFFSD
     YFEPSIISLA WSVMIGGFFQ LFYQFPHLYK IKMLVFPKIN FKNIGLIKVL KKMGPSTLGS
     CANQISLIFN TIFSSLLHSG SISWIYYADR LIEFPIGIIG VSLSTILFTS FSCSYSNNTQ
     SEYKILLNWG IRFGLILSLP ISVILFMFSK PLVIILFQYG KFTDFDVLMT QKALELYSFG
     LVSFILVKIL VSAFYSCQEV NIPMRISILT LFLTQLMNPF LIFYFQHSGL ALSCSIASWI
     NFFLLYWKLY QKGIINFKLN DFIFIFRLLI AVLVMTFFLI FMLYFIPSWK IGSFFDKIIR
     LFTILSISGI VYLIALHFLG IRLLNYSDKL FQKK