ID I3U9Y7_ADVKW Unreviewed; 510 AA.
AC I3U9Y7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Cardiolipin synthetase {ECO:0000313|EMBL:AFK61825.1};
GN OrderedLocusNames=TKWG_06960 {ECO:0000313|EMBL:AFK61825.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK61825.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK61825.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003555; AFK61825.1; -; Genomic_DNA.
DR RefSeq; WP_014749916.1; NC_017964.1.
DR AlphaFoldDB; I3U9Y7; -.
DR STRING; 1036672.TKWG_06960; -.
DR KEGG; aka:TKWG_06960; -.
DR HOGENOM; CLU_038053_1_2_4; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000005267; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:UniProt.
DR CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09112; PLDc_CLS_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..241
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 426..453
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 299..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 59309 MW; E5DD35D4383755B2 CRC64;
MDTAWLASDW FWNTLWALYI IVIGLWVVLQ KRPPVSTLTW ILFLSFVPVL GFVIYYFFGP
KKITRNKINR SISKHLIERD DTLWNVRIQP SDLTEQQRPI HDLALQITHY PLSYATSYQL
LSGGEKTYDR IFDAVRKAEH YIFLEYYIFE QDHTGTTLRD LLTERARQGV KIYLIADAIG
SLRLNRRFMR PLIDAGARLT FFHDISLKHL LSFMNLRNHR KIVICDGTVA FTGGINISDQ
QDRRRNKRAF HDVHLELTGP VVSWLETIFV EDWHYSTHDL SVRHMLREHY RDRLERLQEQ
AEDDADKAPA ARRLANDEQS ADSQPPQETP RWIRTQIIPS GPDFDYASIL RVTVDAIQRA
RHRVYLTTPY FVPDATSAQA LTSASLRGVD VRILLPKRTD NYVVTKAAQS WFDDLVAAGI
RVFEYGPRML HTKSMIVDDD ISFIGSANFD NRSFYLNFEV SVLCYEREAN QALLEEFNAS
MKFAQEVQLT HQPFFSRLSK AVARLFSPLL
//
