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Database: UniProt
Entry: A0A0J8FZ44_CLOCY
LinkDB: A0A0J8FZ44_CLOCY
Original site: A0A0J8FZ44_CLOCY 
ID   A0A0J8FZ44_CLOCY        Unreviewed;       620 AA.
AC   A0A0J8FZ44;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Lipoteichoic acid synthase-like YqgS {ECO:0000313|EMBL:KMT20891.1};
GN   Name=yqgS {ECO:0000313|EMBL:KMT20891.1};
GN   ORFNames=CLCY_1c01250 {ECO:0000313|EMBL:KMT20891.1};
OS   Clostridium cylindrosporum DSM 605.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT20891.1, ECO:0000313|Proteomes:UP000036756};
RN   [1] {ECO:0000313|EMBL:KMT20891.1, ECO:0000313|Proteomes:UP000036756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 605 {ECO:0000313|EMBL:KMT20891.1,
RC   ECO:0000313|Proteomes:UP000036756};
RA   Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT   "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT   HC-1 (DSM 605).";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMT20891.1}.
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DR   EMBL; LFVU01000028; KMT20891.1; -; Genomic_DNA.
DR   RefSeq; WP_048571293.1; NZ_LFVU01000028.1.
DR   AlphaFoldDB; A0A0J8FZ44; -.
DR   STRING; 1121307.CLCY_1c01250; -.
DR   PATRIC; fig|1121307.3.peg.486; -.
DR   OrthoDB; 5901192at2; -.
DR   Proteomes; UP000036756; 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:UP000036756};
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          249..539
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         299
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         473
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         474
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   620 AA;  71009 MW;  5F23D81D9950819F CRC64;
     MNSTQKILKN NLDILLFISI IFLKLISSNI TLKLNGLSFY TIIGCLGSVL VLLGFSYFFT
     KRIRIPIFFV INIIVTLIIY IDNVYNRYFL DVTTIGLIKQ LGITGEVKDS VFNLITIFDL
     LYILDLIILI PFYLKNKREI TRGELKFNKR VISSISMLII GFMLSALSVI GLAKMQVGIL
     NSFYDKKAIV REVGLLNYHV LDINKYINNY MLKKSSITED EKAQVEAFFE NKNKTSLNNP
     KYNGIAKGKN LIVIQLEAFQ SFVLNKKING VEITPNLNKL AKESLNFKNY YFQTSLGGTS
     DAEFLSNTSL LPAREGSVYY QYAQNEYNSL PKSLKESGYY TAVMHANRPG FWNRQEMYKA
     LGFDTFQSEK NYKIDDVKIL GLSDKSFFRQ NIEKLKSYPK PFYGFMISLT SHFSFRDEKN
     SLKDVMNVGE YEGSLVGDYI KTARYTDEAL GQFLNDLKKE GLYDNTVIAI YGDHSAISSD
     KRDQLAKVVY GKETISEFEW QEAQKVVSMI HIPGSNLKGD VDSVAGQYDL YPTLANLFGF
     KTKVTLGQDL LNKSEGFVVT RAGNFVTDSV IYVKAEDKIY DRKTKKELNK KDYQKYFDKM
     NEYFTVTDKI IENNLIKVFN
//
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