ID A0A150H8J2_9MICO Unreviewed; 421 AA.
AC A0A150H8J2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase {ECO:0000313|EMBL:KXZ58419.1};
DE EC=3.5.1.103 {ECO:0000313|EMBL:KXZ58419.1};
GN Name=mshB {ECO:0000313|EMBL:KXZ58419.1};
GN ORFNames=Bravens_01468 {ECO:0000313|EMBL:KXZ58419.1};
OS Brevibacterium ravenspurgense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=479117 {ECO:0000313|EMBL:KXZ58419.1, ECO:0000313|Proteomes:UP000243589};
RN [1] {ECO:0000313|EMBL:KXZ58419.1, ECO:0000313|Proteomes:UP000243589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG56047 {ECO:0000313|EMBL:KXZ58419.1,
RC ECO:0000313|Proteomes:UP000243589};
RA Bernier A.-M., Burdz T., Huynh C., Pachecho A.L., Wiebe D., Bonner C.,
RA Bernard K.;
RT "Use of Whole Genome Sequencing to ascertain that Brevibacterium
RT massiliense (Roux, Raoult 2009) is a later heterotypic synonym of
RT Brevibacterium ravenspurgense (Mages 2008).";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KXZ58419.1}.
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DR EMBL; LQQC01000010; KXZ58419.1; -; Genomic_DNA.
DR RefSeq; WP_062021845.1; NZ_LQQC01000010.1.
DR AlphaFoldDB; A0A150H8J2; -.
DR PATRIC; fig|479117.4.peg.1455; -.
DR Proteomes; UP000243589; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035595; F:N-acetylglucosaminylinositol deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016137; P:glycoside metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.10320; LmbE-like; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993:SF31; 1D-MYO-INOSITOL 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSIDE DEACETYLASE; 1.
DR PANTHER; PTHR12993; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; LmbE-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KXZ58419.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243589};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 296..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 421 AA; 44569 MW; 1C6105163278DA7D CRC64;
MSGVLFVHAH PDDESILTGG TIARLREAQV PVTILTATRG EGGEVIGPLK DTLEGHRDAL
AARREGELAE AMKALGVDDW AFLGTPAGGA GTLPERRFED SGMEWGPDGH AQVPADTPAE
SLCAAKLDDV AAYIAAVIED RRPRLVVTYP AGGGYGHPDH VRVHEATLRA VSRLKRKHRP
RVIYVDTPQE AVDQMFNVDL PGFALTGFEP AQKVPTIPAE APVVLSQDIS AHRGHKARAM
AAHATQLQVA GDFYALSNNI GTVLLDTEYF TSPDGHKGAD ILEFLEEPDR PEPPSAVAMV
FSSVFLGLLA GVLGTFQHLG ASLFNLAGQA VIVPWGLLLA LALAGCVLWY VAEANRSTAA
VVLCAVTMSL VSFIGSQPGL LPGGGVLVTG TLRSVAWLFG PMIIAAVLSF TLPCLRANRK
H
//