ID D8IP88_HERSS Unreviewed; 517 AA.
AC D8IP88;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=mviN {ECO:0000313|EMBL:ADJ62908.1};
GN Synonyms=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN OrderedLocusNames=Hsero_1392 {ECO:0000313|EMBL:ADJ62908.1};
OS Herbaspirillum seropedicae (strain SmR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ62908.1, ECO:0000313|Proteomes:UP000000329};
RN [1] {ECO:0000313|EMBL:ADJ62908.1, ECO:0000313|Proteomes:UP000000329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ62908.1,
RC ECO:0000313|Proteomes:UP000000329};
RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA Weiss V.A., Yates M.A., Souza E.M.;
RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT fixing, plant-growth promoting beta-Proteobacteria.";
RL Submitted (APR-2010) 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; CP002039; ADJ62908.1; -; Genomic_DNA.
DR RefSeq; WP_013233413.1; NC_014323.1.
DR AlphaFoldDB; D8IP88; -.
DR STRING; 757424.Hsero_1392; -.
DR KEGG; hse:Hsero_1392; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_3_4; -.
DR OrthoDB; 9816572at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000329; 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:UP000000329};
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 90..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 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 186..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 387..406
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 412..433
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 445..466
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 486..508
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 517 AA; 56337 MW; F1805C66C7580840 CRC64;
MNLHKTLAAI SGMTMLSRIT GLVREILFAR AFGASAYTDA FNIAFRIPNL LRRLFAEGAF
SQAFVPILAE YKNQRGEQQT KHLVDHVATV LMWVMLVTCV AGILATPFVV YFIATGLQYN
PDAFNASVVM TRIMFPYIGF MAFVALAGGI LNTWKEFKIP AVTSVLLNLA FIIASLFVAP
FMAQPIYAMA FAVLVGGILQ VAIQVPALMK IGMLPHLYWN PLLGLRDEGV KRVLKKMGPA
IFAVSAAQIS LMINTNIASR LEHGSVSWLS YADRLMEFPT ALLGVALGTI LLPSLSNAHA
AQDMEEYSSL LDWGLRLTFM LAMPSAVALA TLSEPLTATL FHYGRFDALS VTMTGHALVA
YGVGLIGLVM VKILAPGFYA KQDIRTPVII AVGVLIATQL MNSVFVPLFA HAGLALSIGL
GACLNALCLF IGLRRRQIYV PRPGWGLFLV RLTGALLVLA GASLWIAGHF DWIALRAHPL
MRIGALALVM LVCALAYFGP LFAMGFRLRE FKRIARR
//
