ID C4FD58_9BIFI Unreviewed; 1227 AA.
AC C4FD58;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Putative integral membrane protein MviN {ECO:0000313|EMBL:EEP21845.1};
GN ORFNames=BIFANG_02241 {ECO:0000313|EMBL:EEP21845.1};
OS Bifidobacterium angulatum DSM 20098 = JCM 7096.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518635 {ECO:0000313|EMBL:EEP21845.1, ECO:0000313|Proteomes:UP000006408};
RN [1] {ECO:0000313|EMBL:EEP21845.1, ECO:0000313|Proteomes:UP000006408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20098 {ECO:0000313|EMBL:EEP21845.1,
RC ECO:0000313|Proteomes:UP000006408};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP21845.1}.
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DR EMBL; ABYS02000003; EEP21845.1; -; Genomic_DNA.
DR RefSeq; WP_003825278.1; NZ_JDTY01000005.1.
DR AlphaFoldDB; C4FD58; -.
DR STRING; 1683.Bang102_001985; -.
DR KEGG; bang:BBAG_1575; -.
DR PATRIC; fig|518635.17.peg.1657; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_004442_0_0_11; -.
DR Proteomes; UP000006408; 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.
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 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 558..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 131589 MW; 0B2515CF06CAECDE CRC64;
MSSSVGRNSL IMASGTLASR VTGQFRTILL AACLGTTGVA ANAYQTGAMI PQVLFTVISG
GIFNAVLVPQ IVRTLKLADA QERLNKLITV SITLLLAMTL LMMASTPLLT MLYLNSNWGP
AQRALVNSFT LWCMPQIFFY GLYTILGQLL AAKDDFAAYA WSSVGANIIS CGGFIAFLCL
FGRANHKPMT FWTTEKVMLS AGTWTLGVAF QALVLFIPLI KLGFKYKPQW GIRGIGLRSM
GPVAAWSLGV MGVQEVANIV NARITNGAPF AGHDMYGIAG NGSYQNAFTL YILPYSLIAV
SIGTAIFPKI SRAVADNNLD EARMDLSVAL RNVGILMMFF TAAYLVMPVQ IIIALLPSVN
LHEAWLIAGP MMMLALGLPL TSAYLLIQRT FFAFEDGMHP FLFQLVMNVI QIVFSLTCMR
ILDPKDWTLC VGLSMTVGYA LSFPLLVIML RRRLAGHLDG RRIAVTYIKT FLAAVVTLVV
GGLFIAPLCN LLQVNLSNYR IGLPWFRAVM FCAVMAVLMA VVYAGMLIVL RCQEFIAMVR
NVVRRFRRTP VVAEAGSDAA SIAANPPADA DDAGDGSADT HDDDTADNAD NAPADEMAGE
SAEKANGLPP QPPESGSRPA SAGNEQPATI SPTKTSQTTV DAAVISTSPA VTITPASTHS
ALQSSAQIGV ENMTKPQLGD TLFNRYTLIA LLRDEPGIQA WKANDRVMAR DCQVFILTAP
QYLESVAASA STLGRAKGFT HVVQFRKAGN AAVLVTNIES GLSLTDYLQG QSGTILSNEA
IRSIIGSAAA LADDLRTPRL STATLRISTN GLEIAGTAIA SMLEEPTQAA GHMQGDQLVI
RQLAALLYAL LTRTPSSKNM TFDLRRLDDT VPSEFRMIIM RGLTMDDGTN HTIPMVSLSE
LTALLGDWTP LDKLSTQDIA LPSTAGEGSI ATAEVISIDE DQLAELPHSI ITTEKLRELT
IEHSPKPRTA SSTPNDRELL RKGEADLSKL ATSTEKTISA VWRKGQEGEE ALKNRLNRPS
KHTNSKEFSN TDLFEDFAFQ ADSEIGTDAN KFDMTTQIPV VDDTNYPTQA IQVSEIQASN
DTPAAQDAAA LPPASFSPAS TSAAQQDAGI AMQQPPSFAP RSKPTADDEG DDLADTRLFG
KYTTATVVVA AAAVVVLLAL GIALACMHFG NNPNNPDSKQ NDWSDSNIDN VPFGNEDGDD
SGKNDSSNSA EGAAGYDYID VTDLFTK
//
