ID A0A1M7QQM4_9SPHI Unreviewed; 2146 AA.
AC A0A1M7QQM4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Non-ribosomal peptide synthase domain TIGR01720/amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SHN33748.1};
GN ORFNames=SAMN05216524_110137 {ECO:0000313|EMBL:SHN33748.1};
OS Mucilaginibacter sp. OK098.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHN33748.1, ECO:0000313|Proteomes:UP000184158};
RN [1] {ECO:0000313|EMBL:SHN33748.1, ECO:0000313|Proteomes:UP000184158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK098 {ECO:0000313|EMBL:SHN33748.1,
RC ECO:0000313|Proteomes:UP000184158};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; FRCM01000010; SHN33748.1; -; Genomic_DNA.
DR RefSeq; WP_073407194.1; NZ_FRCM01000010.1.
DR STRING; 1855297.SAMN05216524_110137; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000184158; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; 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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
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; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 571..646
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1611..1685
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2146 AA; 242026 MW; 665546A1E1201A0F CRC64;
MNLVDVLSKR SEQKSLGITF IESSTQEDFL SYYSLYNSAL KVLSFLQKKG IQPKSELVLQ
IDDNKNFLVV FWACILGGII PVPLSIAKRD DHNKKLSQVW ATLSRPSLII SQNAVKQLEE
YLEEQGLNNQ LQQINSNLLF VEDIFSSDEM GVIHSVEEDD IAFIQFSSGS TGNPKGVMLT
HANLIANVSG IASAAAYTEK DSLLSWMPLT HDMGMIGFHI NPLFSGVNQY LMPTNLFVRN
PRLWLDKICE HKITVTSSPN FGYRYLLKYL NEGAENWDLS SLRIIYNGAE PISEKLCIEF
NEKLAGFGLK DTAMCPVYGL AEASVAVSMS VIENKVQALV LNTQKLNPGD EVQEIDPLLG
SSTFVNVGKS VPGCLVQIAD ENNQTLADGR VGRVKIKGTN VTNGYYNNSS AYDEIIDMNG
WLNTGDLGFI KDGDLYITGR AKDVIFINGQ NYYSHDIEKA AESIEGIELN KIVVISSFVP
ESESEEVIAF LLHRGSLEKL VPVARSLKMC INEKFGFDLT KIIPVKNIPR TTSGKLQRFE
LQKLYKEGEF QQVEQEFTLL FNPFNDNTAV PPANDVEEKI LRIWEDVLQS NNIGVEGKFI
EVGGNSLKAA ELINKLQLAF QVELPIIKLF ELQTVRKLAA EIINLKHKTY EAIPKAALTD
SYPVSAVQKR IYYAWKMDPD SIAYNMPVAI ELEGKVDTEK LTDCLTKLIA RHDALRMTFF
LSEEPRFRVK ESINVQLNII KCEKSEWDDK LKDLISPFDL ANGPLFKFFL LDNENIDDRK
QLLLLDFNHI ISDGQSAYLF INELLQAYQG NVLPTLNASF SDFTTWEQAQ DPGTKEFAKQ
YWAEQLSGEL PVLEIARDFP RPVITSMIGK RQTFSLTESV SAKLKELSTA YQVTKHALLF
TLYRIFLGKY SGQEDVVIGI ASRGRTHPDL QQVQGMFANN LSIRSVVVRN QYFADLLKHA
SKLINNAIDH QDLAFDDLIN FLNIPSRPGR APIFDTMFLY QSLEMSDGQA ADIKFKKYSF
DPGFSKFDIT MEIEDGDQIN YAFEYSTQLF KDKTIIEFSR GFENIIDQVL QNPGVLIEDL
SPLGKREFQD FYVSYNATRK EIEPSVTVLD LFEKQVENNP DAVATEYLGQ QLSYRELDAK
ANQVASALKD KAVGRGDIIG LHLKRSPEMI ATLLGILKTG AAYLPLEQGT PLERVKFIVQ
NSGCTFLISD LEQAHADFAN LPQPEVLTLR SLFDNPGSRF ITQKNQPADL AYVIYTSGTT
GLPKGVMIEH GSLVNYILWA SDEYSNGESY SFAFYSSISF DLTVTSIYMP LTTGNKIVIY
GDDDAAISIN SVIRDNLVDF IKLTPSHLRL IRENNLLSSS SRIKKMIVGG EALDTQLATD
IYEQMQGRVE IFNEYGPTEA TVGCMIYKFK PEDATITVPI GRPIANTQIY LLDSYLKPVP
VNVPGEIYIA GDGLARGYLF LDELTTEKFI ESPFTGGKKM YKTGDIGKWL PDGNLEYIGR
NDKQVKINGN RVEISEIENL LIASGKIKEA VVLVERSKNS NHIQAYFTLI DPGSQLSDIF
FRDYLAEKLP YFMIPGEFVE VETMPLTRNG KIDITALQKF RSLNAGIQKV SAQNEIERVF
VKIWADVLNV AEVGVTDNFF EAGGDSIKAV QISSRLFEEG VVIKVKDILT YHTIKHISQH
AELINDKHSY EQGIAQGQFT PTPIQSWFFK QEFLNPAYFN QSVLFSIKQP LDLTILERTF
QALIEHHDTL RVNYKPVTHS LFYNNDHLKE NHAIAKFKTG DSNSLIDICN DIRSSFDILN
GLLVRMAIIE TDDEHEFLFI TAHHLVMDGV SWRIFLEDFY STYSLLAEGN AVSIPQKTAS
FKEWSSLVNQ LPGSEGIEKE KDYWKMVEET PFTFPQDFHA STTTIRDLKK VAVSLDKETT
EFLLKGAHKS YNTDVPIVLN TALVLALYEL TGLTEFIIEQ ENHGRHLEDI NVSRTLGWFT
TMYPVKLTYQ GEISGLLKSV KETMRNVPNN GIGYGISHFS SDQLRRKPRP SEIRFNYLGQ
FDQELNNRLM AFSKIDSGSE TDPYNAFTTK LEFNAIITDG EFHMEILYSS KLFDHATVNE
LSKCFLACLN HVLAYLKDEK DLYFTPSDFS AVELDEDDIS VLFGDN
//
