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Database: UniProt
Entry: A0A367B0B5_9ACTN
LinkDB: A0A367B0B5_9ACTN
Original site: A0A367B0B5_9ACTN 
ID   A0A367B0B5_9ACTN        Unreviewed;       646 AA.
AC   A0A367B0B5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Murein biosynthesis integral membrane protein MurJ {ECO:0000313|EMBL:RBY93266.1};
GN   Name=mviN {ECO:0000313|EMBL:RBY93266.1};
GN   ORFNames=DQ241_00825 {ECO:0000313|EMBL:RBY93266.1};
OS   Blastococcus sp. TF02A-30.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=2250580 {ECO:0000313|EMBL:RBY93266.1, ECO:0000313|Proteomes:UP000253175};
RN   [1] {ECO:0000313|EMBL:RBY93266.1, ECO:0000313|Proteomes:UP000253175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02A-30 {ECO:0000313|EMBL:RBY93266.1,
RC   ECO:0000313|Proteomes:UP000253175};
RA   Ennis N., Dharumadurai D., Sevigny J., Morris K., Simpson S., Thomas W.K.,
RA   Tisa L.S.;
RT   "Genome Sequence of Blastococcus sp. TF02-30.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RBY93266.1}.
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DR   EMBL; QOHJ01000001; RBY93266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367B0B5; -.
DR   OrthoDB; 9786339at2; -.
DR   Proteomes; UP000253175; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd13123; MATE_MurJ_like; 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   PRINTS; PR01806; VIRFACTRMVIN.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253175};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        138..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        350..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        387..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        474..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        509..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        534..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        573..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        606..629
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..39
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..72
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  66976 MW;  955CEF8058ED2D54 CRC64;
     MPPPPYRARP PADAPFAAPG QDSRPPLPPV PPPVRRPSRP ATGQGPATPD PAATPPPARP
     ARPLPPLPPL RHRWVPAADE TQVFPMPVLP PVPRAPEETD EDVESREERP GASGGILRAA
     GTMAVATLVS RITGLARTMV LTAALGVGLV GDAYTTANTL PNIVYELLLG GVLTSVVVPL
     LVRAQERDRD GGVAYAQRLA TIAMVGLVLM TALAIAAAPL LTALYGLQED PEQYRLANWL
     ARILLVEIVF YGVGALAQAV LNSRGVFGPP AWAPVLNNVV VIATGLVFML AAGPGDLDPL
     TISPGLVWLL AGGTTLGIAV QALVLLPLLR KAGVPLRPRW GLRETGLREA GTLGLWVLAY
     VAVSQVGVIV ATNIANDATR AGGLGSLAFA NATLLFQMPY GIIGVALLTA LVPRMSRAAA
     REDVDGVVAD LSLGTRLSAL GLLPVTALLT VLGPAAAVLL FARGNTTVED AEGIGTALAI
     GAFGLLPMAV TLLQLRVFYA MKDARTPTLI QMGMVAVRVP LLLLVPVVAE PDDVVAGLML
     VTSLTYVAGW VIGDVALRRR LGRLRTAETF GPLLRIAAAS VAAGVLGKLV LIVTDDLRGS
     GTAGSLVTLV LGTVVIGAAA LAGLVVARVP ELREPLERIR ARLGRG
//
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