ID A0A0S6UW05_9BRAD Unreviewed; 508 AA.
AC A0A0S6UW05;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN ORFNames=BDOA9_0157590 {ECO:0000313|EMBL:GAJ36542.1};
OS Bradyrhizobium sp. DOA9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ36542.1};
RN [1] {ECO:0000313|EMBL:GAJ36542.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOA9 {ECO:0000313|EMBL:GAJ36542.1};
RX PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a Symbiotic
RT Plasmid.";
RL PLoS ONE 10:e0117392-e0117392(2015).
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:0000256|HAMAP-Rule:MF_02078,
CC ECO:0000256|PIRNR:PIRNR002869}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02078}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000256|HAMAP-
CC Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
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DR EMBL; DF820425; GAJ36542.1; -; Genomic_DNA.
DR RefSeq; WP_025037460.1; NZ_DF820425.1.
DR AlphaFoldDB; A0A0S6UW05; -.
DR STRING; 1126627.BDOA9_0157590; -.
DR eggNOG; COG0728; Bacteria.
DR OrthoDB; 9816572at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000066441; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd13123; MATE_MurJ_like; 1.
DR HAMAP; MF_02078; MurJ_MviN; 1.
DR InterPro; IPR004268; MurJ.
DR NCBIfam; TIGR01695; murJ_mviN; 1.
DR PANTHER; PTHR47019; LIPID II FLIPPASE MURJ; 1.
DR PANTHER; PTHR47019:SF1; LIPID II FLIPPASE MURJ; 1.
DR Pfam; PF03023; MurJ; 1.
DR PIRSF; PIRSF002869; MviN; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02078};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02078};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transport {ECO:0000256|HAMAP-Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
FT TRANSMEM 24..43
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 270..286
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 307..325
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 345..368
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 380..399
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 405..427
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 439..464
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 476..497
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 508 AA; 54058 MW; 744FC4EC7E473146 CRC64;
MLGRIFTVGG YTLLSRLTGF ARDIMLAAIL GAGPVADAFF VALRLPNHFR AIFAEGAFNA
AWVPAYAHVH GEKGAGAAGL FADRIFTLLL ASQVVLLVVA WLFMPQAMSI LAPGFSEDAE
QRKLAVELTR ITFPYLLLIT LVTLYGGMLN VMQRFASAAA ASIFLNVAMM MTLALAAWFP
TAGHAAAWGV LISGFLQYFL LAGDLARHGG LPRFAPLKLD EDVRGFFKAL GPATLGSMGT
QVALFADTII ATFLPAGALS ALYYADRLNQ LPIGVIGIAI GTVLLPEMSR RITANDHDGA
MQAQRRAFDF TLLFSIPFVA AFLTVPDAIM RALFARGAFS KADAAAAGAT LAAYAIGLIP
FVLIRSAVAA FYARKDTATP VRASLTGIAV NVALKVALMG SLAQIGLALA TAVGVWTNLV
LVLFFAVRRG FLVLDRAWLL SLAKFLLSGL ILAAAFWLIA GFSGPWLGAM HFRDELMLVL
LAVGGTIVYA LAILLLFGRK WLVSLVRG
//
