ID A0A0N0KX21_9MICO Unreviewed; 852 AA.
AC A0A0N0KX21;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=PASTA domain-containing protein {ECO:0000259|PROSITE:PS51178};
GN ORFNames=AEQ27_10955 {ECO:0000313|EMBL:KPG81391.1};
OS Frigoribacterium sp. RIT-PI-h.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG81391.1, ECO:0000313|Proteomes:UP000037934};
RN [1] {ECO:0000313|Proteomes:UP000037934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-h {ECO:0000313|Proteomes:UP000037934};
RA Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-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:KPG81391.1}.
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DR EMBL; LHOZ01000076; KPG81391.1; -; Genomic_DNA.
DR RefSeq; WP_054146675.1; NZ_LHOZ01000076.1.
DR AlphaFoldDB; A0A0N0KX21; -.
DR PATRIC; fig|1690245.3.peg.1034; -.
DR Proteomes; UP000037934; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.30.10.20; -; 2.
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; 2.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 2.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037934};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 704..770
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 773..841
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 463..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 88517 MW; 19FBD1A511F6B40B CRC64;
MSAQKSKPTS AIGALFGFVG FSVLAGLLVT IGVTPAIAVA GMTASSSIGV FESIPEYIEI
GKLQQRNTLY ATQGGQQVPF ATLYSENRVE LSWDEVSPNL KTAVVAGEDR RFYEHGGVDV
TSLVRAAVGS AGAGELGASG GGSTLTMQLV RNIRIAQSQQ LPTADERDAA YKEATTTTLD
RKLEEMKFAI GLEKKYSKDD ILLAYLNIAY FGDQTYGVQA AAQHYYNKSA AELTVPEAAS
LIAIVQYPDS RNMSTPEKYP ANKARRDVII KSMLAEKDID QATADASLAT PVESYVVLTA
PSQGCGAVTV PSAAYFCDYV KKSIKDLAVL GSTPEERQTN WNTGGYDVYT TLNLDLNENA
KAQVDKYAPA TESNFQLGSV VDSVEAGTGR VVVMAQNTTF SETSSPDRTL TSVNYSTDRD
YGGSIGFQPG STYKPFTLID WLEQGHGIYE SVNAKPRTFN MTIDGSRGNK YTPKNDAGEQ
PGQMSVADAT AKSMNTAYAA MAEKLDIADI NGVAKKLGVH RADGGEMHDY ASSILGTADE
IAPLTMATAY AGIAAGGVYC SPIIVDNIKD DKGVDLGGQP QSCSQVVDPQ VAAAAAVAMQ
GLWRNGTGVG GLPADGYPEI GKTGTTDLKD QIWIIGATSK IATAVWQGVA DGPKKSLRSY
NSPNLAGSTS YATARVQYFK AVQSVNNTVY PGGAFGEASG AVLRGSGVAV PDMAGTTPSA
AQALLRGVSL AYEDGGTQPS ALPAGQVIGS DPAVGSVVSK GTTVKVFTSD GSGAAAVPDV
TRQKVGDAVK SIGGAGFDTS KVSVAGFTPG DGKNACQVAS TNPAANTSVA KDSAIGLTVY
GDKDGNDPGN CA
//