ID A0A132T7M2_9MYCO Unreviewed; 831 AA.
AC A0A132T7M2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=AMP-dependent synthetase {ECO:0000313|EMBL:KWX67359.1};
GN ORFNames=ASJ79_21890 {ECO:0000313|EMBL:KWX67359.1};
OS Mycobacterium sp. NAZ190054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX67359.1, ECO:0000313|Proteomes:UP000070146};
RN [1] {ECO:0000313|EMBL:KWX67359.1, ECO:0000313|Proteomes:UP000070146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX67359.1,
RC ECO:0000313|Proteomes:UP000070146};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:KWX67359.1}.
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DR EMBL; LMVQ01000119; KWX67359.1; -; Genomic_DNA.
DR RefSeq; WP_067954839.1; NZ_LMVQ01000119.1.
DR AlphaFoldDB; A0A132T7M2; -.
DR OrthoDB; 8445630at2; -.
DR Proteomes; UP000070146; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000070146};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 588..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..533
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 831 AA; 90711 MW; 4BEA0FE92F0ACD84 CRC64;
MRTLVDHLRG HGDRAAVFTR DQQLSYHDLA ERVEAFARTL GPRRRLVLLE TRNDVTTLVG
YLGALAAGHV VLPVPAGRDH TNIIATYRPD VVVDAAGVHV HSEAARDLHD DLALLMSTSG
STGSPKLVRL SRTNLLANAR SIVEYLQIRE TDRAATTLPM SYCYGLSVIH SHLLAGAALI
LTEQSVADDG FWELFTHHRG TTFAGVPYTF ELLDRVGFQS KHLPHLRCVT QAGGRMPPER
VRKYAALAAG QGWQLFVMYG ATEATARMAY LPPELALTRS NAIGRPVPGG AFTIEPVDEW
AEPGTGELVY RGANVMMGYA HTPADLARGA ELDALRTGDI ARRGEDGLYE VVGRRSRFVK
MYGLRLDLAQ IETTLAGAGV HALCTDNGDR LAVVATDEHD PDDVRRQTAE AAGVPAAVVD
TVCVADLPKL ASGKPDYPTA RVLAAGAARS APRGGDLREV FAEVLLLDPA EIDEDASFVD
LGGNSLTYVT MSARLERALG HLPTDWPQLP LRALRNLPAP KRRRWQSWGH TLETSVALRA
VAIVLIVGSH AELFELWGGA HILLGVAGYN FGRFCLTPLP RPDRIRHLRA TIAWVAIPSV
VWVAFALMVT DDYHASNLLL ANKFLGPHDS MTAGRLWFVE VLVWTLIALA VLFCVPAMDR
LERRHPFGIA MSFLAFGMLL RYGVLAGDTR DAWFTVLAFW FFAAGWAAAK AAHTWQRALV
TAVLFIGLLG YFDDPLRQTM VFAGLALLIW LPAVRCPSGV AAVAAVLAEA SLYIYLTHYQ
VYPLFGSHEL IGVVAALVVG ITVAATVTLA RQWWRDRGVR LPDRARAPAL R
//