ID M4RIV2_9BIFI Unreviewed; 1380 AA.
AC M4RIV2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Integral membrane protein MviN {ECO:0008006|Google:ProtNLM};
GN ORFNames=D805_1837 {ECO:0000313|EMBL:AGH42104.1};
OS Bifidobacterium thermophilum RBL67.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH42104.1, ECO:0000313|Proteomes:UP000011835};
RN [1] {ECO:0000313|EMBL:AGH42104.1, ECO:0000313|Proteomes:UP000011835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH42104.1,
RC ECO:0000313|Proteomes:UP000011835};
RX PubMed=23640377;
RA Jans C., Lacroix C., Follador R., Stevens M.J.;
RT "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT Strain RBL67.";
RL Genome Announc. 1:E00191-13(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP004346; AGH42104.1; -; Genomic_DNA.
DR KEGG; btp:D805_1837; -.
DR PATRIC; fig|1254439.12.peg.1830; -.
DR HOGENOM; CLU_004442_0_0_11; -.
DR Proteomes; UP000011835; 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 CDD; cd13123; MATE_MurJ_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1187..1208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 558..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 147756 MW; 19C25233D053080A CRC64;
MSSSVGHNSF VMAVGTAASR LTGQIRTILL AAAVGTTGMA ANAYQAGSMI PQVIFTLISG
GIFNAVLVPQ IVRTLKEDDA EDRLNKLITF AIALLAGITI AMMLLTATTP AFTHLYANGG
KDMLALTNAF ALWCMPQIFF YGLYTVLGQI LAAKNHFGMY AWSSVAANIV SCAGFTLFIV
MFGKADKQPL SFWTTDKIML TAGTWTLGVA VQALVLFLPL FKLGLRYRWR WGVHGIGLRS
MGSVAAWSLG IVGIDQLLTI ISTRITTNAP LRAHQLFGID ETLVAGNATY QNAFTIYILP
YSLIAVSVAT AVFPKVSRAV ADNDLNTARD DLSDALRNVT LLMSFFSAIF VVLSVPISLA
LLPSISVGEA QLMSGPMIAL SLSLPLSSSY LIIQRTFYAF EDGRSPFIFM AVQLSIQMLT
LLITTKVLSP LDWTLMRGVA VTLAYALSFP LLVWMLRKRF ENRLDGRRIA LSYIKATAAA
VAAAIVGLWL RGPVEHLLGA ELTPSGGHMN WLQSVGVCVV SGIVVIAVYV GALWGMHTEE
LVTMLSSLKA RVASRRSGNA ANVDGDQPAG DTADESADST DTTDTTETAD NRATSGEPNE
PNDSDEPDEP DNPDNPDEPS NPGNRAPDRP RTGPQADSAE DTAVPTAVST TPVVRMTTTT
SPASTRFSRY GAEGTMKPQL GDTVINRYTL VSLLRDEPGL QAWKANDRVL ARDCQLYIVT
DADAIAKVDA IASSLALSRN RRFTQVLQLQ HRGDVSIIIT AVDNGLSLTD YFHGPASGTL
SHAAMRSILG ETASAMRQLL VDGLSHYALN TDTIRLTANG VQLADATLSP MLADTSHAPE
GLGAERLATR QLAAVLYALI TRTPSSVDTQ FDLSKLGPDV PGEFRLICHR GLESDGNGSV
IPMESLAELT ALLGDWEPLS HLQNSDIALP SIDAECSIAN AALKTPVPGH ILDFPQDLSS
SFEQHSYAQA AQASVLPGAS AAIPDAGSNN TDHAEALAAR QQAIQQAMQQ ESAEWMKNSQ
AVPRNPNRQT IPHPEVTDSS DYDFHDIAAA EVANIMAPSV PDPDNAIFPN FNAASGPYTD
TQATMRFDFA RKAAKNAHRL QPPSVNESTS RIPVYDANGV PVLPGDESRR ALENEQTQIL
AANTPVSRPP SFTPTVEPEK ETHEDYNPVT QDDVADEKLF GRFSTKVVAI VVVIVVVAAA
AGLALHSLSG GSTLGAAKQS SAWPSQNLDK VPFGSSTPTS DASSSGSSGK SHIITEDKDA
SAVPTPKVPE NNTPYSIDKQ EFLTKPGGQD GYGYYMHLSE PESVYRFVVS IRSSGGTGYL
YANTTADPTQ GEQVAEFSFD ASGTTDVKLT KTVKSQDFLM WVPRDSLPGN QLYIKSVQLY
//
