ID A0A0R2CSX7_9LACO Unreviewed; 707 AA.
AC A0A0R2CSX7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Sulfatase family protein {ECO:0000313|EMBL:KRM94727.1};
GN ORFNames=FC24_GL000170 {ECO:0000313|EMBL:KRM94727.1};
OS Loigolactobacillus rennini DSM 20253.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423796 {ECO:0000313|EMBL:KRM94727.1, ECO:0000313|Proteomes:UP000051638};
RN [1] {ECO:0000313|EMBL:KRM94727.1, ECO:0000313|Proteomes:UP000051638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20253 {ECO:0000313|EMBL:KRM94727.1,
RC ECO:0000313|Proteomes:UP000051638};
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:KRM94727.1}.
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DR EMBL; AYYI01000085; KRM94727.1; -; Genomic_DNA.
DR RefSeq; WP_057874623.1; NZ_AYYI01000085.1.
DR AlphaFoldDB; A0A0R2CSX7; -.
DR STRING; 1423796.FC24_GL000170; -.
DR PATRIC; fig|1423796.3.peg.178; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000051638; 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 Reference proteome {ECO:0000313|Proteomes:UP000051638};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..550
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 664..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 306
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 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 482
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 483
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 707 AA; 80706 MW; A7957971971D0F9E CRC64;
MTLVWKKLNE LISRRNGFFL LLCGLFWLKT IFAYYVDFSL GVRGLLQHFI LWLNPLATTF
LVLGLGLYIQ RPKWRYWGLL ILSLANTALL YFNVIYYRQF TDFMTINTIL GYSKVSEGLS
GSSLALARPH DIFYWLDLII LMILLLAKLI KINQQPIPRH LPFAVTSFAL LLFSVNLTLG
EANRPQLLTR TFDRNYIVKY LGIDAYTVYD AVKTAQNNQN RAAAKGADLT KVLAFIDQHY
AAPDPQKYGL AKGRNVIIIH LESFQQFLID DKIHGQEVTP FLNHLYHDDQ TFSFPNFFHQ
VGQGKTSDAE NMLETSVYGL PQGSVFTALG SDNTFQAAPA ILGQKGNYSS AVFHGNVGSF
WNRNSVYKNM GYQNFFDANY FKTQGNRSLQ YGLKDKLLFH DSIKYLEQLQ QPFYAKFITV
TNHFPFPLDD EDTDFQLPDT DDKVVNQYFG TAHYLDQALK EFFTYLKSSG LYDNSLILLY
GDHYGLSNKE NLSLAPLLGQ SAETWSSYDN AQLQRVPLMI HLPGQHHGGI QEQYGGEIDV
LPTLEHLLGI DNKGYIQFGT DLFSPHHDQV VAFRNNNFVT PTHTVIGDTI YNHAGDEITH
PSKSLRQKIN RQKKQVRTEL QLSDTVNNKN LLRFYTPVGF KPVAPENYDY KDSLTRLIQA
RQKLGQQSTS VYSKNKNRTT SKTYKSDAPQ LKQTEMQTTP QISTSGQ
//
