ID A0A0K6IVU5_9PROT Unreviewed; 516 AA.
AC A0A0K6IVU5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN ORFNames=Ga0061068_105145 {ECO:0000313|EMBL:CUB07241.1};
OS Tepidiphilus thermophilus.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales;
OC Hydrogenophilaceae; Tepidiphilus.
OX NCBI_TaxID=876478 {ECO:0000313|EMBL:CUB07241.1, ECO:0000313|Proteomes:UP000182108};
RN [1] {ECO:0000313|Proteomes:UP000182108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19170 {ECO:0000313|Proteomes:UP000182108};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02078}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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; CYHH01000005; CUB07241.1; -; Genomic_DNA.
DR RefSeq; WP_055423532.1; NZ_LIPU01000005.1.
DR AlphaFoldDB; A0A0K6IVU5; -.
DR OrthoDB; 5288492at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000182108; Unassembled WGS sequence.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02078};
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:UP000182108};
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 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 87..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 232..257
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 316..345
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 389..408
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 486..504
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 516 AA; 54865 MW; 81702697B9BF8772 CRC64;
MNLLRALATV SGFTLASRIL GFVRDLLIAA VFGAGPATDA FFVAFRLPNL LRRLFAEGAF
SQAFVPVLGH TREREGAQAT QRLIDRVFTL LLAAVSAVTL VGIVGAGALI AVSAPGFLAR
PETFALAVSM TRITFPYILC MALVAFSSAI LNTWGRFALP AATPVALNLS FITFTVLALA
GVPVFEPPVT ALAWAVLVGG LAQVLLHVPA LRRLGTWPRW DWAPRDEGVR RVLRLMAPAV
LGVSVAQVSL LINTVFASLL PSGSVSWLYY ADRLMEFPSG LLGAALGTIL LPSLSRAHAR
ASREDYQALL DWGLRLTVLL TLPAAAGMAL LAEPLVSTLF LHGAFDAQDA LATCRALVAY
SVGLTALIAV KILAPGFYAQ QNVRTPVKIA LVSLVATQAM NGLFVFVLPL AHAGLALSIS
LAAWLNAGLL LHGLWRRGTY RPLAGWGRFL LRVTAATLAL GIVALWGARG LGDWLHLPAL
ERSGRLALLL AACALAYFGT LYASGMRLAE FRRHGA
//
