MURJ_RHITR
ID MURJ_RHITR Reviewed; 533 AA.
AC O05467;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 82.
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;
OS Rhizobium tropici.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=398;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CIAT899;
RA O'Connell K.P., Raffel S.J., Saville B.J., Handelsman J.;
RL Submitted (JAN-1996) 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: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; U47030; AAC32291.1; -; Genomic_DNA.
DR RefSeq; WP_015338622.1; NZ_JAADZA010000001.1.
DR AlphaFoldDB; O05467; -.
DR SMR; O05467; -.
DR UniPathway; UPA00219; -.
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..533
FT /note="Probable lipid II flippase MurJ"
FT /id="PRO_0000182012"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ SEQUENCE 533 AA; 57499 MW; EE1474A35CD0EA5E CRC64;
MSLVKKFITV GGATLGSRIF GFARETLMAA ALGTGPMADV FYAAFRFPNL FRRLFAEGAF
NAAFVPLFAK EIEANGIDGA KRFSEEVFGV LFSVLLLITI VMELAMPLLV RWVIAPGFAD
DAEKFDLTVR LAAVMFPYLM SMSLTAMMSG MLNSLHHFFA AAVAPIFLNL VMISALFYAI
YFGADPLTTA WYLSWSVLVA GVLQLAVVYI GVRHAGISIG LRFPRFTPNV KRLLLLAIPA
AITGGVTQIN LVIGQAIASG KEGAIAALQY ADRIYQLPLG VVGVAVGIVL LPELARSLKS
GHIKEAANIQ NRSIEFVLFL TLPAAVALWL LSDDIIRVLY ERGAFNANNT TLVGSILAIF
GLGLPAFVLI KALQPGFYAR EDTKSPMRYT AIAVAVNSAL SILLFPVLAE RGIALAEAVA
GWLNAVQLFV TLYRRGHLVW EWSLARRTAM LLVSSAVMGG VIVYLSHRWE PLLGSGSTLL
TKTGVLGLLI LIAMAVYFIV AFLIGGVDVG MIRRNLKRKR PAPASDAKAV NGE