ID A0A087B9U9_9BIFI Unreviewed; 1322 AA.
AC A0A087B9U9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Membrane-associated MviN-like protein {ECO:0000313|EMBL:KFI67799.1};
GN ORFNames=BMAGN_1502 {ECO:0000313|EMBL:KFI67799.1};
OS Bifidobacterium magnum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1692 {ECO:0000313|EMBL:KFI67799.1, ECO:0000313|Proteomes:UP000029052};
RN [1] {ECO:0000313|EMBL:KFI67799.1, ECO:0000313|Proteomes:UP000029052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11591 {ECO:0000313|EMBL:KFI67799.1,
RC ECO:0000313|Proteomes:UP000029052};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI67799.1}.
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DR EMBL; JGZB01000007; KFI67799.1; -; Genomic_DNA.
DR STRING; 1692.BMAGN_1502; -.
DR eggNOG; COG0728; Bacteria.
DR Proteomes; UP000029052; 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 Reference proteome {ECO:0000313|Proteomes:UP000029052};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1133..1155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 951..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 142787 MW; 9A7C5178114B81DD CRC64;
MSSSSVGKNS FIMASGTAAS RITGQIRTIL LAAALGTTGL TANAYQAGSM IPQVIYTLIS
GGIFNAVLVP QIVRTLKDKD AEDKLNKLIT FAIVLLAGVT LLMAAMTPIL SRLYVNGNDA
MIALTNAFTL WCMPQIFFYG LYTVIGQVLA AKNHFTTYAW SSVGANIISC AGFGVFLAIF
GHASEQPTSF WTQDKLALTA GMWTLGVAFQ ALVLFFPLMR IGLHYRPRFG VHGIGLRTMG
PIAAWSFGIA IVDQLANILC TRMTTSAPMI AEQQMGLSQY DVAGNATYQN AYTIYLLPYS
LIAVSVATAI FPQISSALAE RKLDEARQDL SSSLRTVGVI MCFFTAAFLV MPLSITRALL
PSVAVPQALL ICAPLMALGI GLPLTSAYLI IQRTFYAFED GRSPFIFMAI YYVLQLGLMY
AGMAFLPPTQ WVMLLGLTGS LGYILSFLPL VLMLRKRFDG SLDGRRIAYA YGKAIVATIV
AVVCGLALRG PIYRMIGIEI HGSTGSMTWI QAVVSAILLT IIITVAYIGV LWILKSEELM
SVLNTVKRRI PGRAAAAAVD EPLNEVEELD APIPTELQQL PADDLDATRV LPQRVTTTTP
TDTLTPDARP ASMPPLYPSP SSVNQQAGEI MRPHLGDTVL NRYTLVSPLR EEPGIEVWKA
SDRVLSRDCQ LFIITNKALL PAVNATAGTL AASHDERFDS VLQLQHAGDI ALVITKIDTG
MSLSQYLRAR TDAPLSYEAM RSIIAEAAQA VMKLQQQHLT HHALGTDTIR LTRSGVQLAD
TTVSAGLVDP SHTDGSVSME RLAICQLGAV LYSMLTRTPS AGVQQFRLSE LPQDTPIEFT
AICRRTLNMT DDEDHPFPLL TMNELHALLE QPKPLIALSR HDVRLTLPTG ECSIVQVPIK
PAKEADILPI PSTLISSSTQ RLAFNGLNLN LPTLPDIDPL IDAAATDGKD LMDAEENGSD
GSSKDDKTGK AGEGAGEKTQ ALKAGESFKA LWDSSKAYME GKDSGTLPEI NPEDATEMFT
AFTGEEPEPP MQPNRMTVPL DVSAIRDGSK DADSGLQATG RIPVFSDTGE IVPPGAESQR
ALDEERRQIN ATYQEGIPAL PPSFTPQETE HTTPVSSQFL PEPKKKHKGR GRVAAIVVVA
VLLACVLGLA IRALATGGSM FDIFKQDSTS YWPKMNLNDV PFGSGKGSDA QAHDDDVKQQ
PSAQPSETQK PENTEPYPIS SGKFLDRPNG QQGYGYLITL DGEHDVNKVV ISIRSSGGTG
FIRVNTNGDP TQGEQVAQFT FDQSGTTTVK LDKSVKTQNV MLWVPLDSLP GNQLYINSMK
AY
//
