(data stored in ACNUC7421 zone)

SWISSPROT: AMJ_BACSU

ID   AMJ_BACSU               Reviewed;         269 AA.
AC   P96581; A7XMW3; Q797M7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Lipid II flippase Amj {ECO:0000255|HAMAP-Rule:MF_02077, ECO:0000305};
GN   Name=amj {ECO:0000255|HAMAP-Rule:MF_02077, ECO:0000303|PubMed:25918422};
GN   Synonyms=ydaH; OrderedLocusNames=BSU04230;
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;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-269.
RC   STRAIN=168 / PY79;
RX   PubMed=18723616; DOI=10.1128/jb.00722-08;
RA   Zeigler D.R., Pragai Z., Rodriguez S., Chevreux B., Muffler A., Albert T.,
RA   Bai R., Wyss M., Perkins J.B.;
RT   "The origins of 168, W23, and other Bacillus subtilis legacy strains.";
RL   J. Bacteriol. 190:6983-6995(2008).
RN   [4]
RP   INDUCTION.
RC   STRAIN=168 / 1604;
RX   PubMed=17434969; DOI=10.1128/jb.00130-07;
RA   Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.;
RT   "SigM-responsive genes of Bacillus subtilis and their promoters.";
RL   J. Bacteriol. 189:4534-4538(2007).
RN   [5]
RP   FUNCTION, PATHWAY, INDUCTION, 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. May serve as a defense mechanism against
CC       naturally occurring MurJ antagonists. {ECO:0000255|HAMAP-Rule:MF_02077,
CC       ECO:0000305|PubMed:25918422}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02077, ECO:0000269|PubMed:25918422}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02077,
CC       ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02077}.
CC   -!- INDUCTION: Transcribed under partial control of SigM ECF sigma factor
CC       (PubMed:17434969, PubMed:25918422). Expression is up-regulated in the
CC       absence of MurJ (PubMed:25918422). {ECO:0000269|PubMed:17434969,
CC       ECO:0000269|PubMed:25918422}.
CC   -!- DISRUPTION PHENOTYPE: Mutants lacking both murJ and amj have a lethal
CC       defect in cell wall synthesis. {ECO:0000269|PubMed:25918422}.
CC   -!- SIMILARITY: Belongs to the Amj family. {ECO:0000255|HAMAP-
CC       Rule:MF_02077, ECO:0000305}.
DR   EMBL; AB001488; BAA19261.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12230.1; -; Genomic_DNA.
DR   EMBL; EU084745; ABU88888.1; -; Genomic_DNA.
DR   PIR; H69768; H69768.
DR   RefSeq; NP_388304.1; NC_000964.3.
DR   RefSeq; WP_003234394.1; NZ_JNCM01000031.1.
DR   STRING; 224308.BSU04230; -.
DR   PaxDb; P96581; -.
DR   PRIDE; P96581; -.
DR   EnsemblBacteria; CAB12230; CAB12230; BSU04230.
DR   GeneID; 938243; -.
DR   KEGG; bsu:BSU04230; -.
DR   PATRIC; fig|224308.179.peg.449; -.
DR   HOGENOM; HOG000089409; -.
DR   OMA; VSRTANM; -.
DR   BioCyc; BSUB:BSU04230-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; 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-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_02077; Amj_flippase; 1.
DR   InterPro; IPR021260; Amj.
DR   Pfam; PF10997; Amj; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P96581.
DR   SWISS-2DPAGE; P96581.
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane;
KW   Peptidoglycan synthesis; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..269
FT                   /note="Lipid II flippase Amj"
FT                   /id="PRO_0000360733"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02077"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02077"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02077"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02077"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02077"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02077"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02077"
SQ   SEQUENCE   269 AA;  29447 MW;  41C4AD7D705D8BB9 CRC64;
     MHVITTQVLF IFCFLLLIHS IETLAYATRL SGARVGFIAS ALSLFNVMVI VSRMSNMVQQ
     PFTGHLIDDA GKNALAIVGE QFRFLIFGST VGTILGIILL PSFVALFSRA IIHLAGGGGS
     VFQVFRKGFS KQGFKNALSY LRLPSISYVK GFHMRLIPKR LFVINMLITS IYTIGVLSAL
     YAGLLAPERS TTAVMASGLI NGIATMLLAI FVDPKVSVLA DDVAKGKRSY IYLKWTSVTM
     VTSRVAGTLL AQLMFIPGAY YIAWLTKWF
//

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