ID   A0A081P0M7_9BACL        Unreviewed;      1294 AA.
AC   A0A081P0M7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Protein SrfAC {ECO:0000313|EMBL:KEQ24250.1};
GN   ORFNames=ET33_11215 {ECO:0000313|EMBL:KEQ24250.1};
OS   Paenibacillus tyrfis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ24250.1, ECO:0000313|Proteomes:UP000028123};
RN   [1] {ECO:0000313|EMBL:KEQ24250.1, ECO:0000313|Proteomes:UP000028123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSt1 {ECO:0000313|EMBL:KEQ24250.1,
RC   ECO:0000313|Proteomes:UP000028123};
RA   Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT   "Draft genome sequence of Paenibacillus sp. MSt1.";
RL   Submitted (JUN-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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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:KEQ24250.1}.
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DR   EMBL; JNVM01000017; KEQ24250.1; -; Genomic_DNA.
DR   RefSeq; WP_036686581.1; NZ_JNVM01000017.1.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000028123; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19543; DCL_NRPS; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 1.10.287.490; Helix hairpin bin; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 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; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028123}.
FT   DOMAIN          979..1054
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1294 AA;  147182 MW;  F523D553187197D8 CRC64;
     MNSKDKIKKI YPLAPSQEGM YYLWLSDKES RQSFVQIKAV LRGELDVPRL EQSMNALVKR
     YDILRTVFVH DNLPRPLQVV MKERKFRLHF EDVSGQAKER QEAYLLQWKQ DNKARGFDLS
     KDLLVRMAVF RTGPQEYRWI WCNHHIILDG WSFARVFREL LDNYRLLQDK REPATVETSP
     YSHYQEWLER QDKKAGIAYW QKTLAGLERS RGGFPVTAQV HSSALDPAGK PAVKPVIMSV
     NAELGQVRME RLQQLARACQ ATINSVFQAG WAIVLRQYVQ SDDVVFGSIV SGRPAEVKGI
     EEMVGLFLNT IPVRIRLQPE QPFAECLKQV QQQALESKAY DFVPLQEMNQ ATDVKHRQLD
     HLMIFENFPF DRRYVDNVES KDGLGFEFAD IRAEEQTEQF NIYVYPQDAA MKFNFNASLY
     EPWLMEQLKD QFVGVLDQIM ADENIPVGRI EVLTPEDKRK LLEGFFQSVR YEQADQTLHA
     CFADQVRKTP DHPALLCGTR TMTYRELHER SNQLAHVLRR RGVQPDDRIG LRVERSVEMI
     TGMLGILKAG AAFVPIPPDY PADRQAYMIA DSGMKLLLTT SPLGEIPFAG ECIDLGDPEL
     DRADRGELLS LSGSRHLAYV IYTSGTTGKP KGVLIEHQGA VNTVLARRAE YPFDGTARVL
     QLYSYAFDAF LSCLFTPLLS GSTVVLATDE EAWNPLALRD HIRDRQVTHL DCVPSVYTAL
     VECLSEEDAR SLRVVTLGGE RLPAKLAKRS REQFPHIELV DEYGPTENSI VTTLERNVVP
     DRPLSIGKPL PNTRVYVLND DRGLVPIGVK GELWIAGRGL ARGYLNLPER TAESFTDDPF
     YPGERMYRSG DLARWLPDGR LEYMGRKDEQ VKIRGYRIEL GEIESVLRSH ERLSEAAVTA
     WDGASGDTVL CAYYVCAAPV SAEELKAFAM ARLPAFMVPT HYTELSRMPL SSNGKIDRWA
     LPQPDVTARE TAEAQAQAVP SNPWEHRLAA VCREILERPE IGVTDDFFEA GGSSLHAMLL
     VSRVQHDYRA ELPLHVILES STIRGMAAFL MDNSKAEPQP IVRLNKKERR KTLFCFPPMG
     GLGIAYYEFA KQMDDCTIYA LDYIDHPDRM DRYVKLITVA QRDGDYTFLG YSAGGNLAFE
     VTKAMEAAGY RVSDVIMLDA YRKTEPEPVT DEALQAMWEG YIATPVIREF YKNFRINELD
     LERLKQYSFY IYLLDNIGTV QADLHVVHST QPEDELRHPP KDEADQQYRN WQGATSGRVA
     YYQGVGGHER MLDPEHMQAN VEIIKGILGS AVVR
//