ID A0A2M9CDQ7_9CELL Unreviewed; 1098 AA.
AC A0A2M9CDQ7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=CDP-glycerol glycerophosphotransferase {ECO:0000313|EMBL:PJJ69995.1};
GN ORFNames=CLV28_2472 {ECO:0000313|EMBL:PJJ69995.1};
OS Sediminihabitans luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Sediminihabitans.
OX NCBI_TaxID=1138585 {ECO:0000313|EMBL:PJJ69995.1, ECO:0000313|Proteomes:UP000231693};
RN [1] {ECO:0000313|EMBL:PJJ69995.1, ECO:0000313|Proteomes:UP000231693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25478 {ECO:0000313|EMBL:PJJ69995.1,
RC ECO:0000313|Proteomes:UP000231693};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC family. {ECO:0000256|ARBA:ARBA00010488}.
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:PJJ69995.1}.
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DR EMBL; PGFE01000004; PJJ69995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9CDQ7; -.
DR OrthoDB; 8549922at2; -.
DR Proteomes; UP000231693; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0047355; F:CDP-glycerol glycerophosphotransferase activity; IEA:InterPro.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11820; -; 2.
DR Gene3D; 3.40.50.12580; -; 2.
DR InterPro; IPR007554; Glycerophosphate_synth.
DR InterPro; IPR043148; TagF_C.
DR InterPro; IPR043149; TagF_N.
DR PANTHER; PTHR37316; TEICHOIC ACID GLYCEROL-PHOSPHATE PRIMASE; 1.
DR PANTHER; PTHR37316:SF2; TEICHOIC ACID RIBITOL-PHOSPHATE POLYMERASE TARK; 1.
DR Pfam; PF04464; Glyphos_transf; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000231693};
KW Teichoic acid biosynthesis {ECO:0000256|ARBA:ARBA00022944};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PJJ69995.1}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 122246 MW; 4B90E5C8C17D46D6 CRC64;
MTAGSSLGTL LGRMRGRPAD DVPAPVTATA RWTPSGLDLA FPPGEDVTEV VVRRVARDAF
GEVSVPVVEA PDGAGRHATV PDAALASLVE DRPRSFAVLA VRASEVPPAD DAEPGLPVHV
ELVDDVERRL PAGPGAVDDA PGARTWTYPG RTGALMVRLA PDGLGPRPRF RVLRVRTSGS
VLRVDGTVEA DATSALVHLE LRAQPSGVVL RSPAVLTAPR RAVPTHRWTH DLTVEADVSA
LVDRCREQGE ELESVQVRLV ESSTPDDPRT VGVGLPRRAR IVPLRELRVS AGDRVALVLP
YQTFKARNLA FRVEHHSRAD HRFLRRLTAV GWAFALARPF ARVWLVGEMP YKAQDTGARY
FEWLRTRHPR RRVYYPIAAD SPERARVEHL GNVVVHGSRR HMVLSLLAQR VVSSHHAEYV
LASRTRAMRR WARGNRVFLQ HGIMGVKNMV LNYGRTAPEF STDRFLVSSE REKEMIVNDF
GYRPRQVAVT GLSRFDRLLA DPVEDPRGVV VIPTWRDWLQ GQAPIEDSEY LLRWREVLED
PRLAGLAAAG HPVTMILHPN MRHHAALFEA PGVTVLRQGD ADVQDLLRSH AALVTDFSSV
ALDFAIQHRP VHYFQFDRPR FLGRRPSHLD LEHDLPGSIH ADAGSLLDAL VAGAASGWTM
SAEHRRRADA LVTHRDTRSC ERIDAAVRST RGPRVAASRL RDGTTGRRLY AVVRRSTAYF
PVAKAAYRVA RLLPRRDTVV LESWNGKKYG DSPAAMYEEL VARGSGLRTV WITSDTFRPR
DPATVKVARL TPRYYWELAR ARYWVSNQNF PHYLAPARGT TYVQTWHGTP LKCMQFDAVS
TTGRDTGYLD RSLRMTGYWT QLLSPSPYAS ARFRSAFRFE GEMVECGYPR NDLLVAGDLA
GTASAVRSRL GLRPDARIVL YAPTFRDDVR SGRGFGVDLP VDWAELVAAL GDDGVLVVRL
HSIVASRLVL PEEVAGRVVD ASAYPDMQEL LAAADVLVTD YSSSLFDFAL LRRPMVFFCY
DLERYRDELR GFYLDPEQDL PGPVVRTSTE LSLALRDALA TPEADRGRIE EFVRRFAPWD
DGRAASRAVD AMLARGTR
//
