ID Q0VQJ0_ALCBS Unreviewed; 678 AA.
AC Q0VQJ0;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Phosphoglycerol transferase {ECO:0000313|EMBL:CAL16558.1};
GN OrderedLocusNames=ABO_1110 {ECO:0000313|EMBL:CAL16558.1};
OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS SK2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL16558.1, ECO:0000313|Proteomes:UP000008871};
RN [1] {ECO:0000313|EMBL:CAL16558.1, ECO:0000313|Proteomes:UP000008871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2
RC {ECO:0000313|Proteomes:UP000008871};
RX PubMed=16878126; DOI=10.1038/nbt1232;
RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA Weidner S., Kaiser O., Golyshin P.N.;
RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT Alcanivorax borkumensis.";
RL Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL16558.1; -; Genomic_DNA.
DR RefSeq; WP_011588393.1; NC_008260.1.
DR AlphaFoldDB; Q0VQJ0; -.
DR STRING; 393595.ABO_1110; -.
DR KEGG; abo:ABO_1110; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_014653_2_0_6; -.
DR OrthoDB; 9760224at2; -.
DR Proteomes; UP000008871; 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; 2.
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:UP000008871};
KW Transferase {ECO:0000313|EMBL:CAL16558.1};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 292..579
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 300
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 340
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 522
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 523
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 678 AA; 76730 MW; 084559FA00B4B79C CRC64;
MTWLKSRRLQ YLLAITALFF SLMVVLRVVF YFGFSEIPSS TTVDSEAVLS ALGIGLRFDL
RLALLIMLPL AALAYLPRFN ILNSGLMRFL AHSYLIIVLV LLGLTYVLDF GHYAYLGERL
NVTALRFLQD TRDSTLMVWE SYPVIWITLG LIAGVAACYW LARIAEHKLL QRPATKISWL
QATAGFLVCF TLFFFAILGR VSNINILNPI PLRWSEAFVS GDRAIGALGL NPVLYFRDTL
VIPVSPFDED KVTEYYPLIA DHLGIPEHQR QDLNFTRMMD VQSHKLDYDR PPNVVFIMLE
SLGASRVSSY GLPVESTPNL DQLGHDGWRF EHFYVPVTGT AKTIWATFTG IPDVAPIESA
SRNPLTSHQR TVLNAFEGYR KFYFIGGNAG WANLDGFVQQ TIDGLELHEE GDWQSPDVDV
WGISDLNLFR ESNQILAELP EDQPFFAFIQ TAGNHRPFTI PENNGDFQAR TDLSDEELAK
FGFRSAAQFN AVRLLDYNVG KYMQWAKESD YFDNTIFVFF GDHSNRITTL PHMPAMDQLE
LESNHVPHIL YAPKYLKPRV IKESVGLVDV LPTIAGMLGL QYPNTTLGRD FQIPAPEGDR
ANFVVLREGP SPIYGMVTKD FLVRMNADGS NATLHDLHSD TPSHDEAAQH PEAFKQLFDL
ARGQYETARY MFYDNVDK
//
