ID E1W159_GLUAR Unreviewed; 543 AA.
AC E1W159;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=MviN-like protein {ECO:0000313|EMBL:CBT77612.1};
GN OrderedLocusNames=AARI_34250 {ECO:0000313|EMBL:CBT77612.1};
OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN [1] {ECO:0000313|EMBL:CBT77612.1, ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RX PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA Vallaeys T.;
RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT adaptation to the surface of cheese.";
RL PLoS ONE 5:E15489-E15489(2010).
RN [2] {ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RA Genoscope.;
RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT CIP 108037 / JCM 13566 / Re117).";
RL Submitted (JUL-2010) 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; FQ311875; CBT77612.1; -; Genomic_DNA.
DR AlphaFoldDB; E1W159; -.
DR STRING; 861360.AARI_34250; -.
DR KEGG; aai:AARI_34250; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_3_0_11; -.
DR Proteomes; UP000006878; 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:UP000006878};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..377
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..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 543 AA; 58050 MW; AEDB69A2632F5D12 CRC64;
MASGTMVSRV LGFVRTAFLA MAIGSVTSVA DIFEKANVIP TIIYMLLAGG IFNVVLIPQL
IKASKAKDRG AAYTSKLVTL TVVGMGILTL ILTLCAKPLI TVLTNNWTEP MIALGTAFAY
WSLPQIFFYG LYAVLGQVLN ANGRFAAFLW APAVNNVIQL IVIGAFILTF GAYSSGDPMQ
DRSSVKTMWL AGGATLGIVL QSVVLFWPLK KTGLKLTLDF QWRGMGLRHV GKLAIWTLAA
MVIGNLSSLV CSKIVSGATA ARTHLPAEQA ASVAGEYALN TSQLITVLPH SLFALTVATV
LFNDFARAFT ENRRKDVGKL LNQGMRSTAI PIVFCTLVFI VLAGPLGRLF AGSSENAAQA
AGALGQLLVL TALGLPFKSL QFFMLRVFYA EEDTRTPMLI QSATAAVGLV LAFLAAALID
PLHIAAAIAF IYGLTNVLTC IGTHYLIKRR YGNYGVSSVI DTYIRVGWMA TLSAGIGVVA
LWLLGGFNFG FAYDSVFTAL ISVAIVAFVM GIVFIGLLYK TKVPELHGFL GPILRRIPGL
KGK
//
