ID A0A077JHD1_9CYAN Unreviewed; 535 AA.
AC A0A077JHD1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=ETSB_0190 {ECO:0000313|EMBL:BAP17078.1};
OS cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake Yunoko.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP17078.1, ECO:0000313|Proteomes:UP000031625};
RN [1] {ECO:0000313|EMBL:BAP17078.1, ECO:0000313|Proteomes:UP000031625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP17078.1};
RX PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA Archibald J.M., Inagaki Y.;
RT "Complete genome of a nonphotosynthetic cyanobacterium in a diatom reveals
RT recent adaptations to an intracellular lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
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; AP012549; BAP17078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077JHD1; -.
DR STRING; 1228987.ETSB_0190; -.
DR KEGG; ceo:ETSB_0190; -.
DR HOGENOM; CLU_006797_5_2_3; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000031625; 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; PTHR43486; LIPID II FLIPPASE MURJ-RELATED; 1.
DR PANTHER; PTHR43486:SF1; LIPID II FLIPPASE MURJ-RELATED; 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|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
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|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 35..52
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 99..123
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 247..272
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 325..351
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 363..380
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 419..443
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 455..477
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 489..510
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 535 AA; 58201 MW; BB1A34D0DCDD2DFE CRC64;
MSNQKKVSRS LFSIASIVAL ATFISKVFGL VREQVIAAAF GVSSIVNAYA YAYVIPGFLL
ILLGGINGPF HSALVSILAK RNKSEAASLV ETVTTLVGII LLMTTIILII FAGTFIDILA
PGLEEQTRAI SVQQLRVMAP LALLAGLIGI GFGTLNAANH YWLPSISPLF SSLAIVISVE
IFTWSVGAQI NSSQYIQLGG MVLAGGTLVG GILQWVVQLI TQSHLGMGKL RLRFDWRTPG
VMDVIRVIGP ATLSSGMLHV NVYTDLFFAS FIQNAAAAMR YANFVALTPL GIISNMILVP
FLPVFSRLTT PENWPELKVR IRQGLLLAAL TMLPLTAIFI AIAPLIIKVI YQRGAFKSTD
VDIVVPVLMA YGLGMFFYLG RDILVRVFYA LGDGETPFKV SVFNIFLNGL LDFLLYKPFA
TPGLVLATIG VNITSMMIFL WILNRRLHGL PLKKWGLSLL GLTAISCMAG AGSWAISLAW
EQLLGSNNLL LQLLQLTLAL GVAFGIFVVL SMQLRLPEVD ILLSRIRHKF NRAYE
//