ID U7LA92_9CORY Unreviewed; 1139 AA.
AC U7LA92;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Integral membrane protein MviN {ECO:0000313|EMBL:ERS55452.1};
GN ORFNames=HMPREF1264_01202 {ECO:0000313|EMBL:ERS55452.1};
OS Corynebacterium sp. KPL1821.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1203560 {ECO:0000313|EMBL:ERS55452.1, ECO:0000313|Proteomes:UP000017152};
RN [1] {ECO:0000313|EMBL:ERS55452.1, ECO:0000313|Proteomes:UP000017152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPL1821 {ECO:0000313|EMBL:ERS55452.1,
RC ECO:0000313|Proteomes:UP000017152};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium sp. KPL1821.";
RL Submitted (OCT-2013) 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:ERS55452.1}.
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DR EMBL; AXLZ01000007; ERS55452.1; -; Genomic_DNA.
DR RefSeq; WP_023020183.1; NZ_KI515751.1.
DR AlphaFoldDB; U7LA92; -.
DR PATRIC; fig|1203560.3.peg.1172; -.
DR HOGENOM; CLU_006797_0_1_11; -.
DR OrthoDB; 9786339at2; -.
DR Proteomes; UP000017152; 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 CDD; cd13973; PK_MviN-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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:UP000017152};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 573..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 956..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 121366 MW; 00719437B9BBFABD CRC64;
MTDKTGREAE HVEKSPAGVV DPKDAAVPAE HPAPAGARGR IVRASPPAPV PEKRPTPAVQ
DTTVPPEKDK SALTGRNAEN ESSNQDVIRA TGTMAIATLL SRVTGFLRQM LIGATLGATV
GTAFSSANQI PNLVTEIVLG AVLTSLVVPV LVRAEKEDTD RGETFVRRLF TLAFSILGIV
TIASVVLAPF LTRMMLPEDS KANAVQATSL AFLLLPQILF YGLFALFQAV LNTKNIFGPG
AWAPVVNNVI SISVLLAYRF LPGQLDPHEP TPVADPHVML LGLGTTTAVM VQCLILLPYL
KKAGINLRPK WGLDARIKQF GGMALAIITY VAISQLGYVI TSRVAAYADA GAPLVYQNAW
LMLQVPYGVI GVTLLTAIMP RLSRNAADGD VDAVVRDLTL GSKLTFIALI PIVIFMTGFG
VPIARALFQY GAYGAESAEQ LGLTISFSAF TLIPYALVLL HLRVFYAREE AWTPTFIIAG
ITLTKIVLTL LAPLMTSNPD RVVILLGTAN GFGFVSGAVI GGFLLKRKLG SLGGKAVTQT
VLWASGAGLV GLVVSWVLYW GVNYLLPENL PSIVSLIKVA VLGVIFLIAT GLVLSKSSLP
EVQNLARALQ RIPGMSRFIK VDSSKAIELE EPDVPEIRPV FTQDAFNATL VPPPMSAGIV
RGPRLVPGAP VSDGRFRLLQ DHGAVTGAQF WQAREQSTGR LVALTFVDTN SLAPIAPSTP
GVAARRSAEI SRNTRRLAEL ELDTVADNIQ VLSYRTGCLV VADWFEGTSL KQVAEADNLD
PHSVARATAP LFADAAAAHD AGLILGVEHR DRFRVSTDGV VKVAFPAVLD GTSAATDREA
LSSALELLVE STEPSPKKLR DISEDANLSA DEAAQRVEDA HFALDSADED SREEKMEQLQ
EAKALTLAGI AQRLHDFAPE EAPEALPVKA EEEPAQEDDP AQEPGFGGRG YSGSGVIVIG
IFATIFVVAM AALTTWIMSL LSDVKASNPV SETIHGSTDI PDTPPVRLQP SSAVTVPDNK
DDAALIDGKT ATTWSTEEED TGILVTVDSP THFAVLPVVQ SNSTGAKYAV YGVNRDRFNP
ENPQAGSLYQ LARGKFKNGK EDIELEKTPE QFDGLLLMIT ELPKSNKATI ADIGLVGQP
//
