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Database: UniProt
Entry: A0A2N7WTI8_9BURK
LinkDB: A0A2N7WTI8_9BURK
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ID   A0A2N7WTI8_9BURK        Unreviewed;       516 AA.
AC   A0A2N7WTI8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   Name=mviN {ECO:0000313|EMBL:PMS32720.1};
GN   Synonyms=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   ORFNames=C0Z20_25410 {ECO:0000313|EMBL:PMS32720.1};
OS   Trinickia symbiotica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=863227 {ECO:0000313|EMBL:PMS32720.1, ECO:0000313|Proteomes:UP000235777};
RN   [1] {ECO:0000313|EMBL:PMS32720.1, ECO:0000313|Proteomes:UP000235777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPY 581 {ECO:0000313|EMBL:PMS32720.1,
RC   ECO:0000313|Proteomes:UP000235777};
RA   Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA   Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA   Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA   James E.K.;
RT   "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT   further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT   gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT   diazotrophy and nodulation in the Burkholderiaceae.";
RL   Submitted (JAN-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PMS32720.1}.
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DR   EMBL; PNYC01000020; PMS32720.1; -; Genomic_DNA.
DR   RefSeq; WP_018440770.1; NZ_PTIR01000021.1.
DR   AlphaFoldDB; A0A2N7WTI8; -.
DR   STRING; 863227.GCA_000373005_02219; -.
DR   OrthoDB; 9816572at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000235777; 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:UP000235777};
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        126..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        157..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        186..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        237..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        278..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        317..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        416..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        445..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        483..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   516 AA;  55130 MW;  85BBAF563586F7D3 CRC64;
     MNLFRALLTV SGFTLLSRVT GLIRETLIAR AFGASQFTDA FYVAFRIPNL LRRLSAEGAF
     SQAFVPILAE FKNSQGHGPT KALVDAMSTV LTWALALLSL VGIVAASAVV FAVASGLKGD
     GQAFGLAVTM TQIMFPYIVF VSLTTLAAGV ANTYGSFSLP AFAPVLLNVS FIAAAVFVAP
     HLKVPVFALA WAVIVGGVLQ FAVQWPGLAK IDMTPRIGLN PFVALAHRGV KRVLMKMVPA
     TFAVSVAQLS LIINTNIASR LGPGAVSWIN YADRLMEFPT ALLGVALGTI LLPSLSKAHV
     DEDPHEYSAL LDWGLRVTFL LAAPSALALF LFAEPLTATL FNYGRFDGYS VVMVGRALTA
     YGVGLIGLIV IKILAPGFYA KQDIKTPVKI GIGVLIATQL GNLVFVPVFA HAGLTLSVGL
     GACVNAILLY TGLRRRGIYI PSGGWALFLV QLLGASLVLA GAMHWCAANF DWIGLHARPL
     ARIALLAACM VLFAALYFSM LWLMGFKYTY FRRRAK
//
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