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Database: UniProt
Entry: A0A1X7IHL8_9MICO
LinkDB: A0A1X7IHL8_9MICO
Original site: A0A1X7IHL8_9MICO 
ID   A0A1X7IHL8_9MICO        Unreviewed;       843 AA.
AC   A0A1X7IHL8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN06296010_0477 {ECO:0000313|EMBL:SMG13750.1};
OS   Agreia pratensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agreia.
OX   NCBI_TaxID=150121 {ECO:0000313|EMBL:SMG13750.1, ECO:0000313|Proteomes:UP000193244};
RN   [1] {ECO:0000313|EMBL:SMG13750.1, ECO:0000313|Proteomes:UP000193244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2510 {ECO:0000313|EMBL:SMG13750.1,
RC   ECO:0000313|Proteomes:UP000193244};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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};
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DR   EMBL; FXAY01000001; SMG13750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7IHL8; -.
DR   STRING; 150121.SAMN06296010_0477; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000193244; 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; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 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   ECO:0000313|EMBL:SMG13750.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          704..770
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          735..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  87840 MW;  347A6F4B45EF9DC0 CRC64;
     MSAQKSKVSG VIGAILGLAG MSAIAGVLVT AMVAPALAVT GIATNNSIGM FENLPSNIRP
     DVLSQKSEIY AKDGAGNPVL LAAVYDQNRE EVGWDQISPF VKDAVVSVED PRFYTHGGVD
     IVSAARAAAQ SAAGGDGPGA STISMQYVRN ILIQKTEEIQ DKAERDKAFE DATKTTVDRK
     LKEMKLAIGL EKEFTKDQIL LGYLNISNFG GTVYGIEAAA QYYYGVSAKD VTLAQATSLV
     AMVNEPNGLR IDQPDQPQKI ADNQARRDVN ILPAMLKEHK ITQAQFDEAK ATPVTPNIVE
     PSTGCTTANA NIGAGFFCDY VSYIVKNDPV FGADADTRWQ KFRTGGFKIF TTLDIDLQTA
     AINSMFENVP KTAAELDLGS SMVTVQPGTG RVLAMVQNKV FNPAEGASPE ETSINFSTDY
     DYGGSTGFPS GSTYKAFTLA QWLKTGHSIN ERVNGSVQTF NLATFKNHCE GSGGGTYKSA
     NDGGPTGSMT VATATANSVN NAFIAMAQKL DMCDITQTAM DFGMHRADGA PLKQVVSSVL
     GINEVAPLTV AAAYAGIAAG GNYCKPIAID QIVDSAGADV PIPPGECKQA VDPNVAATMA
     IPMQQVVANG TATGAQIGDG IPVLGKTGTT DGENHVWFAG ATTALATVIW VGNVQGTTSV
     RYTSIPGYGN VGDMRWPTWT QYMRQANQKF PGVAFPKADG SLTQAPQVAV PAVQGKTIAE
     AQSLVEAAGF TFQDGGATDN EAPAGTAAGT DPAAGTNATK GATVTVYTSN GALKSIPDVI
     SGSNTLGDAA NKLGQAGWKF AGTKYQVTGD GCNEQKPIGT EPAVGSFANP ASQGVYIIGC
     KKK
//
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