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
//