ID A0A0R1HHX5_9LACO Unreviewed; 720 AA.
AC A0A0R1HHX5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Sulfatase family protein {ECO:0000313|EMBL:KRK46205.1};
GN ORFNames=FC66_GL000707 {ECO:0000313|EMBL:KRK46205.1};
OS Dellaglioa algida DSM 15638.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Dellaglioa.
OX NCBI_TaxID=1423719 {ECO:0000313|EMBL:KRK46205.1, ECO:0000313|Proteomes:UP000051450};
RN [1] {ECO:0000313|EMBL:KRK46205.1, ECO:0000313|Proteomes:UP000051450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15638 {ECO:0000313|EMBL:KRK46205.1,
RC ECO:0000313|Proteomes:UP000051450};
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:KRK46205.1}.
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DR EMBL; AZDI01000002; KRK46205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1HHX5; -.
DR STRING; 1423719.FC66_GL000707; -.
DR PATRIC; fig|1423719.4.peg.717; -.
DR Proteomes; UP000051450; 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 GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
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:UP000051450};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..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 253..548
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 669..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 305
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 481
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 482
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 720 AA; 81901 MW; E687A127C23E1B81 CRC64;
MQTLKRLRLF LNTRLGFFTL LLFFFWLKTI TAYLVDFNLG VTGIYQYFVL LLNPIGTTML
LLGLALYIKK PIISYLTMFL IYIANSALLF FNVIYYREFT DFMTINTMLG YSKVSEGISG
SSFALMKPHD IFYVIDLALI ILLFITRYLK FNANPFKKIN AFAIMSFSIM LTLATLTLGE
IDRPQLITRT FDRNYIVKYL GIDSYTVYDS FKTVKNNRVR DTAESYDLNK VLDFTKSHYA
SPNPSMYGVA KGKNVIVIHL ESFQQFLINF KVNGKEVTPF LNSLYNGKQT YSFPNFFNQV
GQGKTSDAEN LLETSIYGLA QGSVFTSLGS ENTFEAAPAI LNQTSGYSSA VFHGNTGSFW
NRDTVYKSMG YQYFFDSSYY DNSAKNTLEY GLKDKLLFND SVKYLERLQQ PFYAKFITVS
NHFPFDIDSQ NKDFEVPNTG DTSVNNYFQT AHYLDESVKE FFDYLQKSGL YNNSMVVLYG
DHYGISNSRN VKLAKLLGKS SETWSSFDNT QMQRVPFMVH IPGINNGGVQ PEYGGEVDVL
PTLLHLLGQD SSSYVQFGTD LFSKTHDQTV AFRNENFITP DYTVLDSTIY DNTTGKEVTH
PSKSVQETIK KEQKKVSIEL NLSDTVNNQN LLRYYTPNNF KPVQPAEYNY KNQYDKLLKL
QQELKNNSTS LYSEKGNKST TNLYKTDAPE LKPASESSSS DSKISSAATS AAHKSNSSSN
//