ID C6X412_FLAB3 Unreviewed; 640 AA.
AC C6X412;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Probable phosphoglycerol transferase {ECO:0000313|EMBL:ACU07150.1};
GN OrderedLocusNames=FIC_00695 {ECO:0000313|EMBL:ACU07150.1};
OS Flavobacteriaceae bacterium (strain 3519-10).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU07150.1, ECO:0000313|Proteomes:UP000001512};
RN [1] {ECO:0000313|EMBL:ACU07150.1, ECO:0000313|Proteomes:UP000001512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3519-10 {ECO:0000313|EMBL:ACU07150.1,
RC ECO:0000313|Proteomes:UP000001512};
RX PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA Raymond J.A., Christner B.C., Schuster S.C.;
RT "A bacterial ice-binding protein from the Vostok ice core.";
RL Extremophiles 12:713-717(2008).
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}.
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DR EMBL; CP001673; ACU07150.1; -; Genomic_DNA.
DR AlphaFoldDB; C6X412; -.
DR STRING; 531844.FIC_00695; -.
DR KEGG; fba:FIC_00695; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_014653_3_1_10; -.
DR OrthoDB; 9777768at2; -.
DR Proteomes; UP000001512; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16015; LTA_synthase; 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 4: Predicted;
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:UP000001512};
KW Transferase {ECO:0000313|EMBL:ACU07150.1};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 270..548
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 324
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 278
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 493
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 494
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 640 AA; 73847 MW; 8E110C364EE04414 CRC64;
MKEFRLQEIA VLFYRIFLAF VFYQIARFLF WMYNKDLIKI DSVSEYLGIA YHGTAFDTTA
ILYVNSLFIL ASLLPLLINT KRNYQKFLLW LYFVLNGIAY AMNFGDFVYY KFSQSRLTMA
AMNVAQNEDN IGRIFLVSVA EHPFVIIWFA ALMSLWVFLY KKVKISERKP RVKWIYFVSS
VVTLCLVATL VVGGIRGDFR HSTRPINLVD ANRHVKNPLQ ANVVLNSVFS FFRTLTTNNF
KEVHFVDEQF INQHIQPYKI YVSKETDPKP NVVIFILESF SKEYSGAFNR DTNIKNFKSY
TPFFDSLAQH SLIATNAYAN GRQSIHGMSS ILAGIPALKD AFTGSPYANQ KIQSIVSVSN
EMGYDTSFFH GAPNGSMGFL GFGNILGFKH YYGKTEYGDD ADFDGMWGIW DEPFFQFFAQ
TLNTKKQPFM ATMFSVSSHH PFKVPQKYEG KFPKGTVEIH APIGYTDYSL RKFFETAKQM
PWFQNTIFVM VADHTNQVAY PEYEKAMNRA AIPIMFYSAN PKYNLRGEIT EPTQQMDIYP
TLADLMGYNR KIRSWGRSLV SEKKEDYLIV NSSGVEHFII GNYIYLFDGQ NVTGIYDKND
LGFEKNLIGT VNSPEIQLGK LKAKAWYQDY MDRVINRKLN
//
