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Database: UniProt
Entry: A0A0Q9LSG1_9MICO
LinkDB: A0A0Q9LSG1_9MICO
Original site: A0A0Q9LSG1_9MICO 
ID   A0A0Q9LSG1_9MICO        Unreviewed;       818 AA.
AC   A0A0Q9LSG1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=PASTA domain-containing protein {ECO:0000259|PROSITE:PS51178};
GN   ORFNames=ASG70_04145 {ECO:0000313|EMBL:KRE56332.1};
OS   Phycicoccus sp. Soil748.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE56332.1, ECO:0000313|Proteomes:UP000051855};
RN   [1] {ECO:0000313|Proteomes:UP000051855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE56332.1, ECO:0000313|Proteomes:UP000051855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil748 {ECO:0000313|EMBL:KRE56332.1,
RC   ECO:0000313|Proteomes:UP000051855};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
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:KRE56332.1}.
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DR   EMBL; LMSC01000006; KRE56332.1; -; Genomic_DNA.
DR   RefSeq; WP_056883046.1; NZ_LMSC01000006.1.
DR   AlphaFoldDB; A0A0Q9LSG1; -.
DR   STRING; 1736397.ASG70_04145; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000051855; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 1.
DR   Gene3D; 3.30.10.20; -; 1.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF03793; PASTA; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00740; PASTA; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51178; PASTA; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          716..780
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          776..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..801
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   818 AA;  86728 MW;  F942ED552A62A5C7 CRC64;
     MSGRATNLGN VVSLLGAFVA SAMVMGLLAA GLLIPAVGAA GSAATSGVKM FDDLPGEFTA
     SALSQQSRIV DAKGNVLATP QQENRIIVNL KDVAPIMRKA QVAIEDSRFY EHGGVDPRGI
     LRAAVSNAQG GDTQGASTLT QQFVKLTLQE NALRNNDEEA AKAAVRVSAA RKIQEIKYAV
     TLEKEMTKDQ ILQGYMNLAY YGDLAYGVEA ASQHYFSIPS AKLNLSQAAL LAGLVQNPSR
     TDPIHFPERA QARRNVVLDR MHDLGIVTDK QWKTAKAVPV KKMLKVKNPV SNCMASSEPY
     FCNYVMEYLK DTSNHGLDAL GKSTPERIKN LTGGGLTIQT TLDATVQAQA RQDVLKKVPF
     ANHALPRDAA DKTKLGLSQM VGSAASIVEP STGRVLAMVQ NSKYPTTKKE QSSYGYTQVN
     WNVDTKYQGT TGFQFGSTAK MFAIVRALET GTPVSGTVPS KFASPTKPAY YSYQEQGPCG
     DPKGWSVHND YAVGGKPIPL KKATADSINT AFASLSMKLG TTKVRDTMTK MHLLQGDGSK
     IGCNPSAVLG TGVVTPLTLA SSYATLANNG KYCPPNPILS ITTADKKPLK IGTPTCKQVI
     DPDVAKGATE LLTGVIKNGT GVRAKLGARP AAGKTGTTDD HVESWFVGYT AQRATAVWVG
     TPYSQQGMRH ITLAGQSYSG VFGGDIAAPI WKDLTEAASQ GLPIRDFDTP SDKILNGDRV
     AVPFVGGMTV EEATARLKEA GFNAQVAGST NSGYSRGIVV YTDPSGTAMR GSTVSLYTST
     GYVPPPPPKS TPKPTSTPKP TATTPKPTKT KKPPPPKK
//
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