ID A0A1I6T8C4_9PSEU Unreviewed; 603 AA.
AC A0A1I6T8C4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative peptidoglycan lipid II flippase {ECO:0000313|EMBL:SFS85197.1};
GN ORFNames=SAMN05660874_03734 {ECO:0000313|EMBL:SFS85197.1};
OS Saccharopolyspora flava.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=95161 {ECO:0000313|EMBL:SFS85197.1, ECO:0000313|Proteomes:UP000198852};
RN [1] {ECO:0000313|EMBL:SFS85197.1, ECO:0000313|Proteomes:UP000198852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44771 {ECO:0000313|EMBL:SFS85197.1,
RC ECO:0000313|Proteomes:UP000198852};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOZX01000006; SFS85197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6T8C4; -.
DR STRING; 95161.SAMN05660874_03734; -.
DR Proteomes; UP000198852; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 63890 MW; 074E36FB4CE24CD7 CRC64;
MNRQDPRLSG GQPDSPTMPM NRDPRQGRPG GHPRQGWHVA ETQPIAAIPA EPGPDQAFEQ
AQTEVIRPVS PGKPSLLKAS GSMAIATLIS RITGFFWKLL LAFAVGFGVV NDSFNVSNTL
PNSIFELLIG GVLTSVVVPV LVRSQKADAD GGQRFVQQMM TLAVVVLGIG TLIAVIAAPL
LTWIFVTASD TSNTELVNVL AYLLLPQIFF YGLSALAGAI LQSKQIFSPP AWAPVVNNLV
VIVTIGVYML LPGEMSLNPV TMTDAHVLVL GIGVTLGVVS QAAIQIPALR STGFTFRWRW
GWDSRLSEFG GLALWMLAYV AVSQIGLVAL SRVAFTGDAG GWSTYNYVWM LLQLPYGVIG
FSIMTAILPR MSAAAADEDY AKVIDDLSLG NRLSTVTLMP VSAVMTALGV PLALSLFALR
GETGSATTLG VALAISAFGV LPYALTMMQM RTFNALNDAR TPTLIMVVMT VAKVLLAVLV
AAILPSDQIV FGLTFVNSFT FIVGWLVGEA WLRHRLGPLG SRRFLATAGK SLIASVIGGL
AAWGVAVGID ALVPGAAGAG TGWLQLLIGS VIGFAVIFGL MSMLRVAELQ PAIGRLTGLL
RRR
//
