PSS_MYCTO
ID PSS_MYCTO Reviewed; 286 AA.
AC P9WPG0; L0T6N4; P96282;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase;
DE EC=2.7.8.8;
DE AltName: Full=Phosphatidylserine synthase;
GN Name=pssA; OrderedLocusNames=MT0452;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK44675.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK44675.1; ALT_INIT; Genomic_DNA.
DR PIR; B70632; B70632.
DR RefSeq; WP_003402213.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPG0; -.
DR SMR; P9WPG0; -.
DR EnsemblBacteria; AAK44675; AAK44675; MT0452.
DR GeneID; 45424397; -.
DR KEGG; mtc:MT0452; -.
DR PATRIC; fig|83331.31.peg.479; -.
DR HOGENOM; CLU_049944_1_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR TIGRFAMs; TIGR00473; pssA; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..286
FT /note="CDP-diacylglycerol--serine O-
FT phosphatidyltransferase"
FT /id="PRO_0000426958"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 286 AA; 31260 MW; E7D56D9ADA740F5C CRC64;
MIGKPRGRRG VNLQILPSAM TVLSICAGLT AIKFALEHQP KAAMALIAAA AILDGLDGRV
ARILDAQSRM GAEIDSLADA VNFGVTPALV LYVSMLSKWP VGWVVVLLYA VCVVLRLARY
NALQDDGTQP AYAHEFFVGM PAPAGAVSMI GLLALKMQFG EGWWTSVWFL SFWVTGTSIL
LVSGIPMKKM HAVSVPPNYA AALLAVLAIC AAAAVLAPYL LIWVIIIAYM CHIPFAVRSQ
RWLAQHPEVW DDKPKQRRAV RRASRRAHPY RPSMARLGLR KPGRRL