MURJ_BACSU
ID MURJ_BACSU Reviewed; 544 AA.
AC O34674; Q795R9;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Lipid II flippase MurJ {ECO:0000305};
DE AltName: Full=Cell division protein YtgP {ECO:0000305};
GN Name=murJ {ECO:0000303|PubMed:25918422}; Synonyms=ytgP;
GN OrderedLocusNames=BSU30050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION IN CELL DIVISION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=19648239; DOI=10.1128/jb.00604-09;
RA Vasudevan P., McElligott J., Attkisson C., Betteken M., Popham D.L.;
RT "Homologues of the Bacillus subtilis SpoVB protein are involved in cell
RT wall metabolism.";
RL J. Bacteriol. 191:6012-6019(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=19666716; DOI=10.1128/jb.00605-09;
RA Fay A., Dworkin J.;
RT "Bacillus subtilis homologs of MviN (MurJ), the putative Escherichia coli
RT lipid II flippase, are not essential for growth.";
RL J. Bacteriol. 191:6020-6028(2009).
RN [5]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=25918422; DOI=10.1073/pnas.1504967112;
RA Meeske A.J., Sham L.T., Kimsey H., Koo B.M., Gross C.A., Bernhardt T.G.,
RA Rudner D.Z.;
RT "MurJ and a novel lipid II flippase are required for cell wall biogenesis
RT in Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:6437-6442(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 (PubMed:25918422). Not essential for growth
CC (PubMed:19648239, PubMed:19666716). {ECO:0000269|PubMed:19648239,
CC ECO:0000269|PubMed:19666716, ECO:0000305|PubMed:25918422}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000269|PubMed:25918422}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Localizes at the septum.
CC {ECO:0000269|PubMed:19666716}.
CC -!- INDUCTION: Expressed at low levels during vegetative growth. Expression
CC decreases significantly during sporulation.
CC {ECO:0000269|PubMed:19648239}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are viable, have no
CC defect in growth, but produce fewer spores, slightly longer cells and
CC show an increase in cell chain formation. Also exhibits some resistance
CC to moenomycin (PubMed:19648239, PubMed:19666716). Mutants lacking both
CC murJ and amj have a lethal defect in cell wall synthesis
CC (PubMed:25918422). {ECO:0000269|PubMed:19648239,
CC ECO:0000269|PubMed:19666716, ECO:0000269|PubMed:25918422}.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000305}.
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DR EMBL; AF008220; AAC00276.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14983.1; -; Genomic_DNA.
DR PIR; G69992; G69992.
DR RefSeq; NP_390883.1; NC_000964.3.
DR RefSeq; WP_003229224.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34674; -.
DR SMR; O34674; -.
DR STRING; 224308.BSU30050; -.
DR PaxDb; O34674; -.
DR DNASU; 937937; -.
DR EnsemblBacteria; CAB14983; CAB14983; BSU_30050.
DR GeneID; 937937; -.
DR KEGG; bsu:BSU30050; -.
DR PATRIC; fig|224308.179.peg.3262; -.
DR eggNOG; COG2244; Bacteria.
DR InParanoid; O34674; -.
DR OMA; FIIIDSG; -.
DR PhylomeDB; O34674; -.
DR BioCyc; BSUB:BSU30050-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd13124; MATE_SpoVB_like; 1.
DR InterPro; IPR024923; PG_synth_SpoVB.
DR InterPro; IPR029303; Polysacc_synt_C.
DR InterPro; IPR002797; Polysacc_synth.
DR Pfam; PF01943; Polysacc_synt; 1.
DR Pfam; PF14667; Polysacc_synt_C; 1.
DR PIRSF; PIRSF038958; PG_synth_SpoVB; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..544
FT /note="Lipid II flippase MurJ"
FT /id="PRO_0000390392"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 544 AA; 59471 MW; 88E46CF4208E0C50 CRC64;
MSSKLLRGTF VLTLGTYISR ILGMVYLIPF SIMVGATGGA LFQYGYNQYT LFLNIATMGF
PAAVSKFVSK YNSKGDYETS RKMLKAGMSV MLVTGMIAFF ILYLSAPMFA EISLGGKDNN
GLTIDHVVYV IRMVSLALLV VPIMSLVRGF FQGHQMMGPT AVSQVVEQIV RIIFLLSATF
LILKVFNGGL VIAVGYATFA ALIGAFGGLV VLYIYWNKRK GSLLAMMPNT GPTANLSYKK
MFFELFSYAA PYVFVGLAIP LYNYIDTNTF NKAMIEAGHQ AISQDMLAIL TLYVQKLVMI
PVSLATAFGL TLIPTITESF TSGNYKLLNQ QINQTMQTIL FLIIPAVVGI SLLSGPTYTF
FYGSESLHPE LGANILLWYS PVAILFSLFT VNAAILQGIN KQKFAVVSLV IGVVIKLVLN
VPLIKLMQAD GAILATALGY IASLLYGFIM IKRHAGYSYK ILVKRTVLML VLSAIMGIAV
KIVQWVLGFF ISYQDGQMQA AIVVVIAAAV GGAVYLYCGY RLGFLQKILG RRLPGFFRKG
RHAG
