ID F8E4Z3_FLESM Unreviewed; 492 AA.
AC F8E4Z3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=Flexsi_0901 {ECO:0000313|EMBL:AEI14563.1};
OS Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Flexistipitaceae; Flexistipes.
OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI14563.1, ECO:0000313|Proteomes:UP000006621};
RN [1] {ECO:0000313|EMBL:AEI14563.1, ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX PubMed=22180813; DOI=10.4056/sigs.2235024;
RA Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Genome sequence of the moderately thermophilic halophile Flexistipes
RT sinusarabici strain (MAS10).";
RL Stand. Genomic Sci. 5:86-96(2011).
RN [2] {ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL Submitted (JUN-2011) 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; CP002858; AEI14563.1; -; Genomic_DNA.
DR RefSeq; WP_013886055.1; NC_015672.1.
DR AlphaFoldDB; F8E4Z3; -.
DR STRING; 717231.Flexsi_0901; -.
DR KEGG; fsi:Flexsi_0901; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_3_0; -.
DR OrthoDB; 9804143at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006621; 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 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:UP000006621};
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 44..66
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..153
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 165..181
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 187..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 272..289
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 309..335
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 355..372
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 384..402
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 439..457
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 492 AA; 54630 MW; A52B37B90052470A CRC64;
MNNFLSKLVK SSSGVLTSRI LGLVRDVAIA AFFGASKFTD AFFMAYAIPN LFRALFAEGA
LSSAFVPIMS DKMHRNPDNA YKYLTDLILV LTFFTLSITA VFIIFSDYAV LLFIPGYLND
PEVIAAASHM LKIVMPYLVI VSICGLLSGY LHVIGSYYIP LSSTAVLNIS MIISAFLGGY
FGGSVTYLAW GALIGGVLQL IYILIYSLIK GFRINRKKRI DKMVKKTFRL IIPSIGGVGI
NQLNFTIGRI IASFLSTGSI SYLYYASRLF QFPLGVFSIA FSTVSLSEIS NSYSRNDLNN
VNKLIDKSVL AIIMVIVPAS LGMFFLSNEI CSLIFEYKIF SSKDTFATAS ALRMYTIGLI
CYSFVNLFTR VYHSVKDTLT PVKFAFISFL ANIAFILIFI NFMGHSGIAL ASSISAGINA
VLLYTSIKYY TFSIKKYKRT VLKIFTSSLL MLIFLLFLKN AGIHVLIIIG LSVCVYFLSL
YMFRVSIRQV LK
//
