ID   MURJ_CHLMU              Reviewed;         536 AA.
AC   Q9PJB9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Probable lipid II flippase MurJ {ECO:0000250|UniProtKB:P0AF16};
GN   Name=murJ; Synonyms=mviN; OrderedLocusNames=TC_0913;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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:0000250|UniProtKB:P0AF16}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000250|UniProtKB:P0AF16}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AF16}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39705.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AE002160; AAF39705.1; ALT_INIT; Genomic_DNA.
DR   PIR; A81650; A81650.
DR   RefSeq; WP_010231926.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PJB9; -.
DR   SMR; Q9PJB9; -.
DR   STRING; 243161.TC_0913; -.
DR   EnsemblBacteria; AAF39705; AAF39705; TC_0913.
DR   GeneID; 1246282; -.
DR   KEGG; cmu:TC_0913; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_497572_0_0_0; -.
DR   OrthoDB; 749401at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd13123; MATE_MurJ_like; 1.
DR   InterPro; IPR004268; MurJ.
DR   Pfam; PF03023; MurJ; 1.
DR   PRINTS; PR01806; VIRFACTRMVIN.
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..536
FT                   /note="Probable lipid II flippase MurJ"
FT                   /id="PRO_0000182003"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   536 AA;  59624 MW;  055D43DC9BF0C439 CRC64;
     MSKDDEGSLV RSLFNLLSGT FFSRLTGMLR EIVMATYFGA DPLVASFWLA FRTIFFLRKL
     LGGPILGLAF IPHFEFLRAQ NISRAAFFFR SFSKFFCYSA IVFTLVIELG LGVWCSCVTG
     SLFDTLLLTI ILLPSGIFLM MYTVNSTLLH CEKKFLSVGL APSVVNVLWI GTVFLARNYN
     PRNRIFGLAI VLVIGFILEW AVTLPGVIKF LGRSTETPKE RDSIRALIAP LSLGLLSMGI
     FQLNLLCDMW LARYINEVGP LYLMYSVRIQ QLPVHLFGLG VFTVLLPAIS RCVQDNEHQQ
     GYDLLRFSLK LTVAVMLVMT MGLLLLALPG VRVLYEHGVF PTTAVHAIVE VLRGYSGSII
     PMALAPLVSA LFYARRNYKV PMLVGIAAAV ANIVLNVIGC LVFKHVSVLA YATSLASWGQ
     LVILWYCAGK SLPTYKGLMW RTFRESGKTV FTTVLAAFIT VGINVFTNTT YIVFIHPLTT
     PIKPLTSLLD QCGVFFAESA LFLAILFGLA KVLKAEDLMN LTSFQYWKGH QSILRN