ID J1F592_9LACO Unreviewed; 722 AA.
AC J1F592;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Sulfatase family protein {ECO:0000313|EMBL:KRN10090.1};
GN ORFNames=FD00_GL000472 {ECO:0000313|EMBL:KRN10090.1};
OS Liquorilactobacillus mali KCTC 3596 = DSM 20444.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1046596 {ECO:0000313|EMBL:KRN10090.1, ECO:0000313|Proteomes:UP000050898};
RN [1] {ECO:0000313|EMBL:KRN10090.1, ECO:0000313|Proteomes:UP000050898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20444 {ECO:0000313|EMBL:KRN10090.1,
RC ECO:0000313|Proteomes:UP000050898};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN10090.1}.
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DR EMBL; AYYH01000014; KRN10090.1; -; Genomic_DNA.
DR RefSeq; WP_003687648.1; NZ_BACP01000064.1.
DR AlphaFoldDB; J1F592; -.
DR PATRIC; fig|1046596.6.peg.501; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000050898; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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 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..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 252..548
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 689..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 304
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 480
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 481
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 722 AA; 81113 MW; BF5919D98B41A73C CRC64;
MYLSKLKKSL SSRFGFFLLL VFLFWLKTIA VYLIDFQLGV TGIYQYAVLL INPIATTVLF
FGCALYIKRT TPAYLTLFLI YIANSALLLF NVIYYREFTD FMTINVIFGY SSVSEGLTTS
SFALLKPQDI IIFIDIILII LGFATRFIKF DRHPIPTKHA AAITSFALFF LVFNITLGEI
GRPQLLTRAF DRNYLVKYLG IDTFTLYDGL KTAKNNQVRN EATSSDLNSI LKFTKKHYAK
ANSSMFGIAK GRNVIVIHLE SFEQFLINFR LNGKEVTPFL NSIYNSKSTY SFSNFFNQVG
QGKTSDAENM LETSTYGLSQ GSLFSSLGTD NTFEGAPAIL NQRAGYSSAV FHGNKGSFWN
RSNVYKNLGY QNFFDASYFN TNANNLTEYG LKDKLLFHDS VKYLERLQQP FYAKFITVSN
HFPYELDSQN TSFKAADTGD TSVDNYFVTA HYLDQAVKEF FDYLKKSGLY DNSMIIIYGD
HYGISNSRNL KLASLLGKSS STWTDNDNLQ MQRVPFMIHL PGTQNGGVQT QYGGEIDVLP
TLLHLLGISS KRYIQFGTDL FSSEHDQVVA FRNENFTTPK YSVVNGNIYD NSTGLQITHP
SASLAAKIKK ESAKVNTELT LSDTLNNKNL LRFYVPKGFT PVNPKNYNYK DDFGEISKIQ
KILGKKSTSL WSKNGNKTTI SDYVSDAPEL KTTDDNAKNV SSAVASTKNS SSISESSSSS
GD
//
