ID A0A2A5NUM3_9MICO Unreviewed; 533 AA.
AC A0A2A5NUM3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=MOP family protein {ECO:0000313|EMBL:PCN48985.1};
GN ORFNames=Csp2054_04230 {ECO:0000313|EMBL:PCN48985.1};
OS Curtobacterium sp. 'Ferrero'.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2033654 {ECO:0000313|EMBL:PCN48985.1, ECO:0000313|Proteomes:UP000218649};
RN [1] {ECO:0000313|EMBL:PCN48985.1, ECO:0000313|Proteomes:UP000218649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ferrero {ECO:0000313|EMBL:PCN48985.1,
RC ECO:0000313|Proteomes:UP000218649};
RA Osdaghi E., Forero Serna N., Bolot S., Fischer-Le Saux M., Jacques M.-A.,
RA Portier P., Carrere S., Koebnik R.;
RT "High-Quality Draft Genome Sequence of the Curtobacterium sp. Strain
RT 'Ferrero'.";
RL Submitted (SEP-2017) 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:PCN48985.1}.
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DR EMBL; NXIA01000003; PCN48985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5NUM3; -.
DR OrthoDB; 9786339at2; -.
DR Proteomes; UP000218649; 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 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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 533 AA; 56286 MW; 5DD173D7B59CB03F CRC64;
MLAAGTMVSR VLGFAKTIIL AYAIGQQGSV AADAFAVSNQ LPNNIYALIA GGLLSAVLIP
QIVRSMQQHT DGGTAYVNKI VTLGGSLFVV ITVIATVLAP VLVRLYSTQA GDGSKGFSPA
QTDLAVAFAF WCLPQILFYA MYSLLGEVLN AKQVFGPFTW APLINNVIAV AGLIVFMALF
GDRSVNAGLD DWTPAKIAVL AGSASFGVVA QAAFLPFFWR RAGLTFRPDF RWRGVGLKAT
GTAAGWLFAM ILVTQLAGLV QSRVSSLGTG AAGNAVLQNA WLLFMLPHSI ITVSIATAYF
TRMSHDAERG DLDAVRRNLS LSLRIVGLFT VFASVALMVV SVPFGRIFAS TFDGALSIGA
VLLAYMPGLV LFSMLFIIQR VFWALHDHRT PFLMQCVQSA LFVIGALAVS LLPGEAIGFA
IAACTTLAGS TQTVVALVLV SRRLRGMEGP NVLRSHLQFI VAAVVAGVVG LGVVWFFGAF
TPSGFAMADA TGAVLTILLT GAVMALVYFG VLALARNQEI RGAVDIVRAR LGR
//