ID A0A2T0TSW2_9MICO Unreviewed; 755 AA.
AC A0A2T0TSW2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Cyanophycin synthetase {ECO:0000313|EMBL:PRY48618.1};
GN ORFNames=BCF74_1494 {ECO:0000313|EMBL:PRY48618.1};
OS Knoellia remsis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=407159 {ECO:0000313|EMBL:PRY48618.1, ECO:0000313|Proteomes:UP000237822};
RN [1] {ECO:0000313|EMBL:PRY48618.1, ECO:0000313|Proteomes:UP000237822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1496 {ECO:0000313|EMBL:PRY48618.1,
RC ECO:0000313|Proteomes:UP000237822};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY48618.1}.
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DR EMBL; PVTI01000049; PRY48618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0TSW2; -.
DR Proteomes; UP000237822; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR041656; TPR_5.
DR PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF12688; TPR_5; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000237822}.
FT DOMAIN 189..401
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 426..506
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT DOMAIN 631..750
FT /note="Tetratrico peptide repeat group 5"
FT /evidence="ECO:0000259|Pfam:PF12688"
SQ SEQUENCE 755 AA; 79543 MW; A187842F17229124 CRC64;
MPSDTSPATT VTEPRDAASS AVAWSAADPA GVTATEVRVL EGPNLYFPRP AVKVTLDLTA
YADADKDTVR DIARAAGLRA AQVGAPGSEQ RQRVLARLAE RAVRRLSQAS GTRRLGVRAR
PSSDRASVVV AFVWRRRGPA QVLGEAVAPV LSAWLNGHDV VEEYAVRVRS AEPGAPARIV
TPQVPVASVT GTNGKTTTTR LLAHIAMTAG RHTAWSSTDG VVDHGTMIEP GDYSGPAGAR
GVLGAPGVEI GILETARGGM LLKGLGVTHN DVSVVTNVSA DHLGLQGVDT VDQLAEVKAI
ITRATRPEGW TVLNGDDPRV WAMRTGSPAK PWVFTLDPNS PAIREALGAG GRAITVLDDR
ITVLDDSGIP DRLVRVTDVP MTIAGLSRHN VANVLGAAAA ALGLGIERDA VVEGLRTFQP
DASLNPGRMN TYSVPTGTGG ACTVVVDLAH NEAGLEALLD VATGLRAPGA RVLLGLGAGG
DRTDEILENL GEIAGLRADQ VVIVHKEHYL RGRSREDLEG RFRDGLQRAG VADVPAFPTE
VDGLRALVDS AHDGDVVALM CHSERAEVYA WLESSGGTPD DAATIRRKVV AARGEHEAEE
AIAALWADDD AQRRIATAAD LYAAHPGDAR IAYEYAGTFD SAGEEARAVG LYREALDAGL
REPHRHRAVI QLASSLRNVG EHDEALRLLD ELAVDRPDSV GIAGFRALAL HSAGRTTEAL
SSLLGIVAKA STDEDVARYR RSLTAYAEEL DPPRD
//