ID A0A345HSD5_9ACTN Unreviewed; 602 AA.
AC A0A345HSD5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Murein biosynthesis protein MurJ {ECO:0000313|EMBL:AXG79609.1};
GN ORFNames=DVK44_20320 {ECO:0000313|EMBL:AXG79609.1};
OS Streptomyces paludis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282738 {ECO:0000313|EMBL:AXG79609.1, ECO:0000313|Proteomes:UP000253868};
RN [1] {ECO:0000313|Proteomes:UP000253868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSSD-12 {ECO:0000313|Proteomes:UP000253868};
RA Zhao J.;
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 ---------------------------------------------------------------------------
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; CP031194; AXG79609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345HSD5; -.
DR KEGG; spad:DVK44_20320; -.
DR OrthoDB; 3695748at2; -.
DR Proteomes; UP000253868; Chromosome.
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 InterPro; IPR004268; MurJ.
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:UP000253868};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 60859 MW; 79495E30AD77D0FF CRC64;
MTDTRRSALP APPATVVPAQ TPPPEVESGT GSLTSGPAGR FLARAALVTA LLTAAGSVLG
LVRDQTIAHL YGAGPGTDAF LVAWTIPEVS ATLLIEDAMA LILVPAFSFA LARRAAAVPG
TAADPVRLLT RSTLPRLFLA LSAAAALLAV AAPWVVALLA PGLPETQLAV DCTRLTATSV
FTYGLAGYCS AVLRAHGSFV APAAIYVASN VGIIGTMLVV RDRWGVEVAA GGVAVGGVLM
VLIQLPCLWR RLAEGRQTAG AGADSVGGTA AVAQGTPATA TATASVTATA TATATATATT
TAAATAPVAL GLLAPVIVFA LSRQSQVLIE RFLAAPLPAG AISHLNYAQK VAQIPMTLSL
MLCTVTFPVV ARAMAAGETD RARRRVERDL ALAGAIVLVG AATIIACAPQ FIEVLFQRGE
FTAADTAATA AVMRVYALGL LGHTLVGALV RCYFSAARPL WFPAVAMIAG LGLTTVAGSL
LVQVWGVRGI AAANALGITL TAALMLAGLA RHSVPLDARF MAGGLTKLSA AAAAATGAGW
LCGALVASPA PAATAACAVI AAVFLVLARA LRAPEIDSLL DPVLRVLRTL LRPASRKPPH
VR
//