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Database: UniProt
Entry: A0A0N0KX21_9MICO
LinkDB: A0A0N0KX21_9MICO
Original site: A0A0N0KX21_9MICO 
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
//
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