ID A0A2M9HNB2_9BIFI Unreviewed; 1327 AA.
AC A0A2M9HNB2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Virulence factor protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CUU80_10135 {ECO:0000313|EMBL:PJM78312.1};
OS Bifidobacterium scaligerum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2052656 {ECO:0000313|EMBL:PJM78312.1, ECO:0000313|Proteomes:UP000228755};
RN [1] {ECO:0000313|EMBL:PJM78312.1, ECO:0000313|Proteomes:UP000228755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRED {ECO:0000313|Proteomes:UP000228755};
RA Mattarelli P., Modesto M., Bonetti A., Puglisi E., Morelli L.;
RT "Draft genome sequences of strains TRE 1, TRE D, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (NOV-2017) 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:PJM78312.1}.
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DR EMBL; PGLQ01000011; PJM78312.1; -; Genomic_DNA.
DR OrthoDB; 9786339at2; -.
DR Proteomes; UP000228755; 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 Reference proteome {ECO:0000313|Proteomes:UP000228755};
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..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..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 291..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..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 1092..1110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 556..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1327 AA; 141093 MW; AA73CB763EEC5067 CRC64;
MSSSVGRNSL IMASGTAASR ITGQLRTILL AAAIGTTGLA ANAYQAGSMI PQSVFTLVSG
GIFNAVLVPQ IVRTMKEEDA QERLNRLITL AIGLLLAMTL LMTVCAPLLT MLYVGGGDHQ
MMALTTAFTL WCMPQVFFYG LYTVLGQILA ARDHFATYAW SSTGANVISC AGFTAFIMLF
GKANEQPLDF WTADKIALTA GTWTLGVAFQ ALILFVPLAR LGFKYRPSFG LSGFGLKAMG
PVALGSLGVV IASELCGIVL SRVTTMAPQY AHELTGASLF TVAGNATYQN AYTLFILPYS
LIAVSVSTAI FPKISRAVAD NNLDEARHDL GSALSNVGLL LMFFGAAMVV FPEPIIRALL
PSVSMNETML ISYALVALAI GIPMGAAFLL IQRTFYAFED GLHPFLSALV QYTITAVLIV
AGTTMLPPEH WVTWSSYAVT ISSLVALPVM VTMLRKRFGG YLGGRAIALT YGKALAAAVA
AGAVTWLVKQ PLTVLFGVRI QPVGGHMSWF SAIGICVVLT AVLFVVYVAM LWALRTPELN
VFVRSLRARF GRFGAGAADG AAPDASAAAT EVRDAASPES MPADTSTDHH GSADPTDSAK
PNASSSLSMS SPRTMRKASP TDRMSTLRFN TTNNRTESDE PMKPHLGDTI LNRYTLVSSL
REEPGLEAWK ANDRVLARDC QLFIISDRGA FAAVNELAGQ ITANKPNRVS PVLKYRMESG
VMLIIMPLDE GQSLTEYFGD AGKPLSYSAM HSILGECTDV MRSTLTSASN LAINTDTVRV
TTSGVQIADA PCTPMIVDTC GVTAQDSPER HAIRQLAALL YAMLTHAPVR AGQTFDLGQL
PADTPGEFRV ICKRGLELSE SDETTLPMAT LVELEALLGD WKPLNELDGA DIALSSIEGR
SSIGTAALKP VEPAHIVAMP STLVDRTQLP ELSIGAAGAA AGIAGAAGVA GGAVPLPEGK
QDARRLFDFN LSDAWQHENL SGEDTGDWYN EMNPAPTGGP GDNSRLTVPI AVGGLSDTTV
GETTSRIPVF DASGREVMPG EESLRALEEE QARIAEVSAV PPSFEPKETA GNTRADNKLP
DEHLLGTFTT KAVAIVVALV LVIAAAFWAV HAFQSSGVNP ADPQSNTAEG EWPDIDTNDV
PFGSNTSGDN TDSTSSDTST DSSSNSTKSE STDTSTSTEK NQSKSDQTDT SDSQQSTSKK
KTTADKDAKA VPTPRHVNNT AYTIASANFL TNPGGQQGYA YHLHLDQAHD VYRMTVTIRT
SGGTGYIRAN TTEDPTKGEQ VAKFTFAEGG TTEVKFDKTI NTQDLILWVP VDSLPQNQLY
IQKVEVF
//
