ID A0A117PUR1_9ACTN Unreviewed; 487 AA.
AC A0A117PUR1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Poly-gamma-glutamate synthase PgsB {ECO:0000313|EMBL:KUM93123.1};
GN ORFNames=AQI88_28825 {ECO:0000313|EMBL:KUM93123.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM93123.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM93123.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM93123.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUM93123.1}.
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DR EMBL; LMWL01000052; KUM93123.1; -; Genomic_DNA.
DR RefSeq; WP_067004712.1; NZ_KQ948032.1.
DR AlphaFoldDB; A0A117PUR1; -.
DR STRING; 67285.AQI88_28825; -.
DR OrthoDB; 2884at2; -.
DR Proteomes; UP000054241; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR008337; Capsule_biosynth_CapB.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR NCBIfam; TIGR04012; poly_gGlu_PgsB; 1.
DR PANTHER; PTHR43445:SF1; PGA SYNTHASE CAPB; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR PRINTS; PR01758; CAPSULEPROTB.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054241}.
FT DOMAIN 41..200
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT REGION 450..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 53632 MW; 823012978439A600 CRC64;
MLFLYVIVLL CCTALWIAGI LEQRRHFASL EQIPTRVLVN GIRGKSSITR LCAGALRGGG
LVTVSKTTGT AARFIHPDAT EEPVYRKFGI SNIVEQIGIV RRAATYRPDA LVIECMAVMP
ALQEINQEKL IRSTIGVLCN VREDHLEEMG PTLDDVARSL SRSMPVGGVC VTAEKDRLHI
LQEEADKRNC QLIAVDPESV TDAELRGFSW FTFKENVAIA LAVAELLGVE RQTAMQGMWD
APPDPGVLSV ERYVTPEGKR LRFANVFAAN DPESTLMNVK QLEDLGAIRR PIGVVINCRP
DRVERNGQMG TIVPDLAAET VFLIGHPTKS ARDAIPDGFT GRVVDLGGDR RDPEELTAAI
LAELGPDSSL VAIGNIHGQG ELFLECLADL PLDDSEDLFD AVPDGDGLDQ ETMQIAIPRP
RVSVARPPEP EPYSWVAPLE TPTYAFRIPE QRELAHRFAD RQGRPDDQST ADDPQHSYDP
YQFTRNP
//
