PSS_MYCBO
ID PSS_MYCBO Reviewed; 286 AA.
AC P59949; A0A1R3XVB9; X2BEX8;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase;
DE EC=2.7.8.8;
DE AltName: Full=Phosphatidylserine synthase;
GN Name=pssA; OrderedLocusNames=BQ2027_MB0444C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; LT708304; SIT99030.1; -; Genomic_DNA.
DR RefSeq; NP_854107.1; NC_002945.3.
DR RefSeq; WP_003402213.1; NC_002945.4.
DR AlphaFoldDB; P59949; -.
DR SMR; P59949; -.
DR GeneID; 45424397; -.
DR PATRIC; fig|233413.5.peg.484; -.
DR OMA; IRRAQPH; -.
DR Proteomes; UP000001419; 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_0000056796"
FT TRANSMEM 15..35
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