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Database: UniProt
Entry: D7CJB0_SYNLT
LinkDB: D7CJB0_SYNLT
Original site: D7CJB0_SYNLT 
ID   D7CJB0_SYNLT            Unreviewed;       528 AA.
AC   D7CJB0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   OrderedLocusNames=Slip_0208 {ECO:0000313|EMBL:ADI00999.1};
OS   Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophothermus.
OX   NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI00999.1, ECO:0000313|Proteomes:UP000000378};
RN   [1] {ECO:0000313|Proteomes:UP000000378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX   DOI=10.4056/sigs.1233249;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA   Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H.;
RT   "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT   C1T).";
RL   Stand. Genomic Sci. 3:267-275(2010).
RN   [2] {ECO:0000313|EMBL:ADI00999.1, ECO:0000313|Proteomes:UP000000378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX   PubMed=21304731;
RA   Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT   C1).";
RL   Stand. Genomic Sci. 3:268-275(2010).
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 membrane {ECO:0000256|HAMAP-Rule:MF_02078};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02078}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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; CP002048; ADI00999.1; -; Genomic_DNA.
DR   RefSeq; WP_013174403.1; NC_014220.1.
DR   AlphaFoldDB; D7CJB0; -.
DR   STRING; 643648.Slip_0208; -.
DR   KEGG; slp:Slip_0208; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_006797_4_1_9; -.
DR   OrthoDB; 9804143at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000378; Chromosome.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000000378};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        51..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        87..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        129..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        313..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        351..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        410..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        450..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        480..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   528 AA;  55410 MW;  41296352290EFBA9 CRC64;
     MGTINNTAGT VARAAAVIVI FTGLSKILGF IREMVLAYGF GAGAATDAYL VALTIPGIIF
     AILGGALAAG AVPLFTSFRS RWGEDEAWRL FSAMITFLLV VLTGFTLAGE PLARQLVWLI
     TPGLPEETAV LAASLTRIVL PSVIFLALGN IYYGLLNANG IFGPPAFSSV LTNVLVIGGL
     VLGMKYGIVA AAWGVLSGYA AAFLLQVPYM RGVGFRYRPV WDLKHPGMLE AWQMLVPVLI
     SSGLGQIYLI IDRILASGLP EGSITALNYA QKVAMLPQGM LAVPLATAIF PALAERAVAE
     SEEDFARALT RGVSLILVTT LPLAVLVLVL ARPTVELLFM RGAFDERAAV MTTLALAMFA
     IGLVGQCVNP LMTRGFYARQ DSVTPLKCGV VAIGLNLVLS LILIHPLKHA GLALANSLAA
     TFNVFQLGWR LSRMSGGQVS FSGIGRDVGM TVVAAAVCGL AAWACDAVLA GMVGMGTVGA
     FIRVAVAGSI GLVVFGTVAW FLRVREFVAL VEKGVGLLQR RPSTGSVN
//
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