ID G5K3U6_9STRE Unreviewed; 725 AA.
AC G5K3U6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Arylsulfatase {ECO:0000313|EMBL:EHI69916.1};
DE EC=3.1.6.- {ECO:0000313|EMBL:EHI69916.1};
GN ORFNames=STRIC_1468 {ECO:0000313|EMBL:EHI69916.1};
OS Streptococcus ictaluri 707-05.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764299 {ECO:0000313|EMBL:EHI69916.1, ECO:0000313|Proteomes:UP000003330};
RN [1] {ECO:0000313|EMBL:EHI69916.1, ECO:0000313|Proteomes:UP000003330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=707-05 {ECO:0000313|EMBL:EHI69916.1,
RC ECO:0000313|Proteomes:UP000003330};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004936}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the LTA synthase family.
CC {ECO:0000256|ARBA:ARBA00009983}.
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:EHI69916.1}.
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DR EMBL; AEUX02000006; EHI69916.1; -; Genomic_DNA.
DR RefSeq; WP_008089552.1; NZ_AEUX02000006.1.
DR AlphaFoldDB; G5K3U6; -.
DR STRING; 764299.STRIC_1468; -.
DR eggNOG; COG1368; Bacteria.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000003330; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16015; LTA_synthase; 1.
DR Gene3D; 3.30.1120.170; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012160; LtaS-like.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR47371; LIPOTEICHOIC ACID SYNTHASE; 1.
DR PANTHER; PTHR47371:SF3; PHOSPHOGLYCEROL TRANSFERASE I; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:EHI69916.1};
KW Manganese {ECO:0000256|PIRSR:PIRSR005091-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR005091-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000003330};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..558
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 696..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 310
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 490
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 491
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 725 AA; 82475 MW; 8D75953A681879EF CRC64;
MKKFKTLITG FISTRLGFVL TLLFCYWLKT LWAYHTDFSL DLENLYQVFL TIINPIPLAL
LLLGFALYIK NTRVFYIAAW IAYIILNLLL ISNSIYYREF SDFITVSAML ASSKVSAGLG
DSALNLLRIW DIVYILDFII LITLTVTKTF KKDRRPFNKR ASFAITALSF LLLSINLFLA
EIDRPELLTR GFSNTYIVRA LGLPAFTLYS GNQTYQAQKE RNGATAEELV DVKDYVKEHY
AAPDPQYFGI GKGKNVVVLH LESFQQFLID YKLKDNDKEY EVTPFINSLY HSNETLAFSN
FFHQVKAGKT SDAETMMENS LFGLNSGSFM VNYGGENTQF ATPNILAQDG GYTSAVFHGN
VGTFWNRNNA YKQWGYNYFF DSSYFSEQNS KNSFQYGLND KYMFKDSIKY LEQLQQPFYT
KYITVSNHYP YTSLKGERDE EGFPLAKTDD ETINGYFATA NYLDAALKSF FDYLKATGLY
DNSIFVLYGD HYGISNSRNS SLAPLLDKDP ETWSEYDNAM LQRVPYMIHI PGFKNGGIKD
TFGGEIDSLP TLLHILGIDT THLVQLGQDL LSPQNSQIVA QRTSGTYMTP EYTNYSGRLY
STQTGLEITN PDEMTMAKIK EIKDATARQL AVSDAVQTGD LLRFDSKNGL KVVDPSEFVY
TKQLKHMKAI SEKLGSHSTS LYSKNGNKST QKIFKAPSYL ELNPKENEET AYPPTEKDIN
QKTKE
//
