ID D1AKC9_SEBTE Unreviewed; 494 AA.
AC D1AKC9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=Sterm_2191 {ECO:0000313|EMBL:ACZ09045.1};
OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Sebaldella.
OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ09045.1, ECO:0000313|Proteomes:UP000000845};
RN [1] {ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA Woyke T., Wu D., Eisen J.A.;
RT "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ09045.1, ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX PubMed=21304705;
RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Chen F.;
RT "Complete genome sequence of Sebaldella termitidis type strain (NCTC
RT 11300).";
RL Stand. Genomic Sci. 2:220-227(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001739; ACZ09045.1; -; Genomic_DNA.
DR RefSeq; WP_012861639.1; NC_013517.1.
DR AlphaFoldDB; D1AKC9; -.
DR STRING; 526218.Sterm_2191; -.
DR KEGG; str:Sterm_2191; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_3_0; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000845; 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:UP000000845};
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 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 48..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 305..323
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 435..456
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 494 AA; 55859 MW; AFC48CBAE4096A43 CRC64;
MFKSSLLVMI INMLSRILGL VREILIGSFF GATGMTDAYF GAFKISNFFT QLLGEGALGS
VFIPLYNEKR ELEGKDKADD LIFSVLNLVF AFSTTVSIFM IFFSEYMLKI FVGFKDEARF
NVANNLLKIM AFYFLFISLS GIVSAVLNNF KKFVISTSTA LVFNLTIICG VLLFGKKYGI
YGLGVSVLLS GLFQLLMQLP QFFMIVKRYK LIFDIKDKYI REMFLLMIPT LIGIFGYQIN
EMIDTRFAAA LTAGTVSALN YSSRLYLLPI GVFAISLSVV IFPNLSQAAV KKQMNVVKSQ
IERGLNMLAF FVIPSQIVLI FYSKEIVSLI YKRGAFSEDM IVVTSQALTF YSVGLLFFST
IHLLTRSHYV FKDRKRPVIS SFVGIGINIA LDFLLYKQYK HMGLTFATST AAMVNYLILL
LSLNKNYIKL DFLKYIKFIV ITLIISGIAY IVSSFIPEIG DFRISIVIKL IIFAVVYLLL
WSPKIIKQKI NMFG
//
