ID H6SLJ0_PARPM Unreviewed; 775 AA.
AC H6SLJ0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00014944};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
GN ORFNames=RSPPHO_02229 {ECO:0000313|EMBL:CCG08855.1};
OS Pararhodospirillum photometricum DSM 122.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Pararhodospirillum.
OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG08855.1, ECO:0000313|Proteomes:UP000033220};
RN [1] {ECO:0000313|EMBL:CCG08855.1, ECO:0000313|Proteomes:UP000033220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA Duquesne K., Sturgis J.;
RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC the acidic phospholipids. {ECO:0000256|ARBA:ARBA00003973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001566};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005042}.
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}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR EMBL; HE663493; CCG08855.1; -; Genomic_DNA.
DR AlphaFoldDB; H6SLJ0; -.
DR STRING; 1150469.RSPPHO_02229; -.
DR KEGG; rpm:RSPPHO_02229; -.
DR PATRIC; fig|1150469.3.peg.2505; -.
DR eggNOG; COG0558; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_360883_0_0_5; -.
DR OrthoDB; 9796672at2; -.
DR Proteomes; UP000033220; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1760; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR NCBIfam; TIGR00560; pgsA; 1.
DR PANTHER; PTHR14269:SF60; CARDIOLIPIN SYNTHASE (CMP-FORMING); 1.
DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR Pfam; PF13185; GAF_2; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000033220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 289..439
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT DOMAIN 582..650
FT /note="Signal transduction histidine kinase
FT dimerisation/phosphoacceptor"
FT /evidence="ECO:0000259|SMART:SM00388"
FT REGION 185..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 84767 MW; 8D29E11CF7CBB757 CRC64;
MLTLPNVLTL ARIVVIPVMV ALFYIDAPAA RWVNGTLFIA AAITDFFDGW LARRSNQVSR
LGRFLDPIAD KLLVAAVLMM LVGVGHISPW SYPAAVVILM REILVSGLRE FLAEIQVIMP
VTRLAKWKTT VQLVALAVLI LGPLPGLGLP VSLLGELLLW VAATMTLITG YDYLRLGLRY
MGPEHDQPAP PKKSGAHVPL TPPAPDAPPV NEGPGEAAPP QFFVILALSL SRPWAGAIGE
TMSERPEASA PSQTGEETAL SLLHSAPLAL THFMTWQKRI VTSLLRTRDL QTTLETLVHL
IEDLNPGVLC TVMRLSDNRL FFAAGPSFPD FYHEAVDGVE IGEGVGSCGT AAFRGETVIV
ENLYSHPYWA NFRGLMSAVG VASCWSEPVR THEGRILGTF ALYRRKPHIP SAQELEQIKV
FADLTAIFME FCAADQTRQI TEQRLLHVVA DIPGALYEFR LTRDGTMSLP FLSEGIRRLT
GHALGPVVPD ARALLMNIAT GDRRAALLDS ILHSAQTLTP WASDLPLPGD DGPRWLRCEA
RPRRHPDGSV VWAGVMTDIT RDKQKAQQDH ATTTALAQTN AALEGFVTTA AEDLSDPLRM
IAGFLALLRR RLAPVMDEET REVIDFAVEN AQRLEDHVGT LLAYTQSQNE PEAVVALDTV
LAESLTLLCT RHPRVNERLR VETPLPSVVG RKTQLILVFQ AVLEAFLRPP FTGVTLRTRE
GESDWEITFA SADLRVSGDL PLGLAMARHI LTAHQGSLSL EAGRATLRLL KKGEG
//
