ID A0A2B8BJR1_9PROT Unreviewed; 1137 AA.
AC A0A2B8BJR1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acyl-[ACP]--phospholipid O-acyltransferase {ECO:0000313|EMBL:PGH57773.1};
GN ORFNames=CRT60_07270 {ECO:0000313|EMBL:PGH57773.1};
OS Azospirillum palustre.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2044885 {ECO:0000313|EMBL:PGH57773.1, ECO:0000313|Proteomes:UP000225379};
RN [1] {ECO:0000313|Proteomes:UP000225379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2 {ECO:0000313|Proteomes:UP000225379};
RA Kravchenko I.K., Grouzdev D.S.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PGH57773.1}.
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DR EMBL; PDKW01000039; PGH57773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8BJR1; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000225379; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR CDD; cd06173; MFS_MefA_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50850; MFS; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:PGH57773.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:PGH57773.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..424
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 1137 AA; 117886 MW; 6E7B333C06F0B121 CRC64;
MNASALLASR RFLPLFLAQF LGAFGDNVLR GAIAVLAVYG VSGEGALSGA MISTLAAGAF
TLPFLLLSAT AGQLADRYDR TVIARIVKLA EIGLMAVASL GIVAADLPVL IVALVGMGAH
STLFGPVKYG LLPDLLDPSE LTAANGLVEA GTFVAILLGT IAGGSLALLH PWAVPGMLGA
SALLGLAASL FIPRAGNADP AVAVGLNPLA VTVRVLRSVA GDRASMRAIH GISVFWGVGA
VVMAQFPSIA RETLGTDSGG ATLLLAVFAI GVAAGSVYAG LSHRTPSTAD AGRAALAGLV
AALAGAALPL LTPATPALEP LSPLALLAQP WALPLLADLF VIAAAGGAFA VPLYALIQHR
AAPGARARVI AAAYVVNALY MVAGSAVAAG MLALGASPLT VASVGGASMA VAVVMALAVD
AQALMRAVFR GLFRLAFRVE VRGAEHLTTL DGAAVVTPNH QSFLDGALLA AFLPGMRFAV
DTHIAKHPLV KPFLAIADHV TIDPTNPLGT RILARALADG DKVCVFPEGR ITVTGSLMKI
NGGPGMLADK ARCPVVPVCI EGAQRSILSR MKGRLRLGLF PHITITVLPP VTTPDVGGLV
GKKRRAALKS WLSRVMTESV FAARPRQETL MLALLDARAK AGAREEAVQD GDFSTLSYRA
LAARALVLGR ILTRGTEADE PVGVLLPTAS PTAAVFFGLA AHGRPAAMLN FTAGPDAVKA
ACRAAGVRRI VTSAQFIEKA RLGALVEALA ADHAIIHLEE VKRGLRLGDK LRALAALVAP
DRLLPPQGNS DDIAAILFTS GSEGPPKGVA LSHGNLLANM AQVASVVDFN RQDVVFNCLP
VFHSFGLTGG MLLPILNGVK TVLYPNPRHV RLIPELVYQT NATVLFGTDF FLNAWARSAD
PYDYRSLRLV FAGAERLQDE TRRVYTEQLR VHLLEGYGTT ETAPVIAVNT PARFRPGSVG
QALPGIETEL LPVPGVDAGG RLRVRGPNVM QGYLHADRPG VIQPPQDGWH DTGDIVEIDA
DGFIRIVGRV KRFAKVAGEM IPLGLVEELA GLADPDATHA AVALPDAKRG ERIVLATTGT
ALTRDALVAA ARARGAPEIA IPRDILRIDA VPLLGTGKTD YPAVTRFAAE AAAKEPA
//
