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Database: UniProt
Entry: A0A0C2B9N0_9ACTN
LinkDB: A0A0C2B9N0_9ACTN
Original site: A0A0C2B9N0_9ACTN 
ID   A0A0C2B9N0_9ACTN        Unreviewed;      1357 AA.
AC   A0A0C2B9N0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE   Flags: Fragment;
GN   ORFNames=QR77_37895 {ECO:0000313|EMBL:KIF78035.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF78035.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF78035.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF78035.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) 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:KIF78035.1}.
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DR   EMBL; JTHL01000001; KIF78035.1; -; Genomic_DNA.
DR   STRING; 1576605.QR77_37895; -.
DR   OrthoDB; 2472181at2; -.
DR   Proteomes; UP000031584; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd12117; A_NRPS_Srf_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01720; NRPS-para261; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 2.
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   SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584}.
FT   DOMAIN          777..851
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KIF78035.1"
SQ   SEQUENCE   1357 AA;  145994 MW;  BDA3418D014482EF CRC64;
     FWKRTLRDLP EQLELPVDFP RPAVASHVGG SVRVSVPAGV HARLVELSRG SGATAFMVVQ
     AALAVLLSKM GAGEDIPIGT PVAGRTDDAL DDLVGFFVNT LVLRADVSGD PSFREVLERV
     RERDLAAFAH QDVPFERLVE ILNPTRSMAR HALFQVMLTF QNNTRPDLDL PGIHAEVEPL
     KSAAARFDLS FNLGETHTDD GTPAGLEGEL NYRTDLFAEA TVEVLADRLV RVLEAVVADP
     DQPVRAIDVL GEEERRRTLV AWNDTAHEVP EASLPELFRA QVTRTPDALA VISDGAELTY
     AELDARAEEL AHGLNARGVG SRDRVALLLG RWIDQVSMTL ALTRVGATYV PLDNRSPAAR
     LEFILGDTSS VAVVVDRETL ALIPEQNPYG IDVLAVDELP TGRPPAATGT APQVRPLDLA
     YIMYTSGSTG RPKGVAVSHR NVVALVSDRY WERAAADRVL LHSSPSFDAS TYEMWGALLT
     GATLVAPAGV AADIPELART MGESRVTVGL FNEGIFRLLA ESEPESFSSL RDVYVGGDTM
     SRAAVRKVRG QASRMRLTNS YGPTEATLCV AHYALPSETD DWASIPIGRP LDNTRLYVLD
     KGLKPVPPGV VGELYVAGEG LARGYVDRPD LTAERFVADP FGPAGARMYR TGDRAKWRRD
     GILEFAGRTD DQVKVRGFRI EPGEIEAALE SYANVAQAVV IAREDRPGDK RLVAYLVAAT
     GARIDADATR LRLAEVLPDY MIPAAFVRVD ALPLGATGKL DRSALPAPDY SGGGRQAPRT
     EKERVLCEVF AEVLGVDQVS ADDNFFAMGG DSIVSIQLVA KARAAGLIVT PRSVFERKTV
     EALAAVAVES DERTAAGEDL GVGPVPLTPV MHQLRERGGS VDRFSQSVTL VAPAGLDRDD
     LTAAVQALTN HHDLLRARLN TTSADGAWQL EVLPPEALSA ASCVSRVEVA GIEGVELRQA
     VAEQEDEARS FLSPSDGRML RVVWLDAGPR RHGRLVVTVH HLAVDAVSWR ILVPDLVAAW
     QDIVSGRKPE LQPVYTSFRR WADHSSAEAE RRVGELPLWE GVVADAGGAL SGFARSLDPA
     HDTWGTARSV TVTLPADLTS ALLTSLPDAF NCGPDSVLLA AFLLAVGASD AQRQGSEPAV
     VVDVERHGRE QVSPALDVSR TVGWFTSVAP VRLDLKSVSN GRTTVENDAE AALKHVKEQL
     RAAPDNGFGY GMLRYLNPRT AERLSRFPEP GILFNYLGRI PVPAGGETPE EPWSVVGDGE
     VGAGADPRMA MAYSLTINAV ARETAEGSEL LTTWAWPGRM WDEEGVRGLA EAYTHALTSL
     AALAEAPGVG GLTPSDVSLL TLSQDEIDEF ELGEIED
//
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