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Database: UniProt
Entry: Q1Q214_KUEST
LinkDB: Q1Q214_KUEST
Original site: Q1Q214_KUEST 
ID   Q1Q214_KUEST            Unreviewed;       539 AA.
AC   Q1Q214;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078,
GN   ECO:0000313|EMBL:QII11084.1};
GN   ORFNames=KsCSTR_17050 {ECO:0000313|EMBL:QII11084.1}, KSMBR1_0829
GN   {ECO:0000313|EMBL:SOH03340.1}, kuste3293
GN   {ECO:0000313|EMBL:CAJ74053.1};
OS   Kuenenia stuttgartiensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Candidatus Kuenenia.
OX   NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ74053.1};
RN   [1] {ECO:0000313|EMBL:CAJ74053.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16598256; DOI=10.1038/nature04647;
RA   Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA   Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA   Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA   Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I.,
RA   vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M.,
RA   Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D.,
RA   Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA   LePaslier D.;
RT   "Deciphering the evolution and metabolism of an anammox bacterium from a
RT   community genome.";
RL   Nature 440:790-794(2006).
RN   [2] {ECO:0000313|EMBL:CAJ74053.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SOH03340.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH03340.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000221734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Frank J.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QII11084.1, ECO:0000313|Proteomes:UP000501926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSTR1 {ECO:0000313|EMBL:QII11084.1,
RC   ECO:0000313|Proteomes:UP000501926};
RA   Ding C., Adrian L.;
RT   "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT   Kuenenia stuttgartiensis genomes.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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; CT573071; CAJ74053.1; -; Genomic_DNA.
DR   EMBL; CP049055; QII11084.1; -; Genomic_DNA.
DR   EMBL; LT934425; SOH03340.1; -; Genomic_DNA.
DR   KEGG; kst:KSMBR1_0829; -.
DR   OrthoDB; 9804143at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR   Proteomes; UP000501926; 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:UP000221734};
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        87..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        125..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        156..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        235..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        376..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        433..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        464..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        506..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   539 AA;  60200 MW;  C54397513BD7E852 CRC64;
     MSDIKKLIYS VKTISSCTFL SRILGLGRDI ICASIFGTGL VWDAFTVAFK IPNLFRRLFG
     EGALSAAFIP VFTEHIEKHG EREAWKFANI VITLLIIILG GIVFIGEGSF FVVPKLFNIH
     EKWQLIFKLL IILFPYVFFI CIVAFMGAIL NTVRHFFIPA FAPMILNICW ISGAFVSFYT
     GNVTEKMVFT VAIAILFSGI IQMYVHLPFL RQKGFNYRPS FQFTHPGLKS VFTRMAPIVF
     GLAIVQLNVL LDSIIAVGFA STSDGQGSFA FAGMNIPFPL KVGAASVLYY SDRLIQFPLG
     VFGVAMATAV FPFFSTYAAR EDWENFSRTF NKALKFILFM GIPASIGIIM LREPIVSLLY
     KRNQFDAESA LRTSRVILFY AIGIWAYCGL HVLIRAFYSL KDTVTPVKIG TLCVGLNLVL
     NISLIWTLQE GGLALSTSIS AIIQIIILTL ILQKKLSIKI QKEVFVSLVK TIIISVAMGF
     VCFFTLKMLP YSEENTSLYF KGIRLFIPML TASATFAVAS FLIKSEDFRN LIKGVLKKP
//
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