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Database: UniProt
Entry: K8ZMN9_9ENTE
LinkDB: K8ZMN9_9ENTE
Original site: K8ZMN9_9ENTE 
ID   K8ZMN9_9ENTE            Unreviewed;       716 AA.
AC   K8ZMN9;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Lipoteichoic acid synthase LtaS Type IIc {ECO:0000313|EMBL:EKU27813.1};
GN   ORFNames=C683_0278 {ECO:0000313|EMBL:EKU27813.1};
OS   Catellicoccus marimammalium M35/04/3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Catellicoccus.
OX   NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU27813.1, ECO:0000313|Proteomes:UP000016057};
RN   [1] {ECO:0000313|EMBL:EKU27813.1, ECO:0000313|Proteomes:UP000016057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU27813.1,
RC   ECO:0000313|Proteomes:UP000016057};
RX   PubMed=23405330;
RA   Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., Santo Domingo J.W.;
RT   "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT   Commonly Found in Gull Feces.";
RL   Genome Announc. 1:E00019-12(2013).
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:EKU27813.1}.
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DR   EMBL; AMYT01000008; EKU27813.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8ZMN9; -.
DR   STRING; 1234409.C683_0278; -.
DR   PATRIC; fig|1234409.3.peg.249; -.
DR   eggNOG; COG1368; Bacteria.
DR   Proteomes; UP000016057; 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; 2.
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:UP000016057};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..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..555
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   REGION          661..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        309
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         309
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         486
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         487
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   716 AA;  82322 MW;  5FD27C653D1D8260 CRC64;
     MKKFSLKKVL NTRMGYFALL ALITWLTNIY AYFTTFNLGI QSPFQYFILI INPIATTLLL
     LSIGLYCKKG KTAYILMTTI AILMNILLFS NVVYYREFSD FITVNSILGV GSVASGLKSD
     IFKLIHPHDI VYWISYIVIF ILFATKYLKV DQRPLPKRVA FAMSSLAVFI FGANLTLAEI
     DRPELLSRTF SHDYMVKYLG INAFTTYDGI QTYKIDQRRA QASEMDLTRV EKYVKDHYAA
     PNPKYFGMAK GRNVVVIHLE SLQQFIIDYK YKDKDGKQYE VTPFLNKLFH DKQTFAFDNF
     FHQVGSGKTS DAETLMENSL FGLSQGPIMV QLGGKNTFQA APNILKQNGN YTSAVFHGND
     GTFWNRNEAY KHFGFDYFFD SSYFDLNPSN SFQYGLHDKY MIKDSIKYLE RMQQPFYVKF
     LNVSNHYPFA PFKGKESGFP IADTGDDTVN GYFATANYLD EAVRELFDYF KKSGLYDKSI
     FILYGDHYGI SNTRAKNALS PLLGKSPETW TDFDDMQMQR VPYMIHIPGQ DKGFIDHTYG
     GQVDNLPTIL HLLGINTKNY IELGQDLFSK ENQQIVAFRN GNYVTPQFTS IDGEVYSNKT
     GKPIKKPTKK QQKTINYDAK QVEEQLQVSD EINNGDLLRF ANNGIKPVDP SQFNYKDQME
     RLQKEEKEKG KDSTSVYNKN HNQSTTSLFQ SKSYQELHGK TKYSTSENSK DKEEEK
//
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