ID A0A0A2WKZ1_BEABA Unreviewed; 2405 AA.
AC A0A0A2WKZ1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BBAD15_g340 {ECO:0000313|EMBL:KGQ13744.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13744.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ13744.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13744.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ13744.1}.
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DR EMBL; ANFO01000024; KGQ13744.1; -; Genomic_DNA.
DR STRING; 1245745.A0A0A2WKZ1; -.
DR HOGENOM; CLU_000965_1_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
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; cd02891; A2M_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 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; IPR049120; A2M_bMG2.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR049122; A2MG_CUB.
DR InterPro; IPR040639; A2MG_MG1.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR InterPro; IPR041203; Bact_A2M_MG5.
DR InterPro; IPR041462; Bact_A2M_MG6.
DR InterPro; IPR041246; Bact_MG10.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR40094; ALPHA-2-MACROGLOBULIN HOMOLOG; 1.
DR PANTHER; PTHR40094:SF1; UBIQUITIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF21142; A2M_bMG2; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF21765; A2MG_CUB; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF17970; bMG1; 1.
DR Pfam; PF17973; bMG10; 1.
DR Pfam; PF11974; bMG3; 1.
DR Pfam; PF17972; bMG5; 1.
DR Pfam; PF17962; bMG6; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF07678; TED_complement; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000313|EMBL:KGQ13744.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2405
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001996387"
FT DOMAIN 758..906
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 969..1060
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 2405 AA; 263166 MW; 2E333DA696905906 CRC64;
MNALRLTSLA ALVCGLLALS GCDDKNNQQT GQPTASAAAE QNGKAETKPD AAQLEKLAQQ
SAGKPLKLLD ASEVQLDGAS TLVLTFSIPL DPNQDFNKVA HLVDKTSGKV DGAWELSSDL
KELRLRHLEP KRTLIVTVDS GLLALNKATF DDSFEKQIAT RDIQPSVGFA SRGSLLPTKV
IAGLPVMALN VDKVDVNFYR IKDSSLSGFV SQWQYRNSVS NWESDNLLKL ADLVYTGRFD
LNPARNTREK LMLPLGDIKP LQQPGVYLAI MNQAGHYAYS NAATLFTLSD VGVSVHRYHD
RLDVFTQSLE NGAAQSGVEI ALLNEKGQTV GQTKSDGDGH ATLEKLNKGT LLLARNGEQT
TLLDLSRPAL DLAEFDIAGE QGYSKQFFMF GPRDLYRPGE SVIVNALLRD GDGKPLPPQP
VKLEVVKPDG QVARTEVWQP ANGLYQFTWP LSESAATGNW QVRVNTGDNQ PRSWIFKVED
FMPERMALNL TAQSQPIAPE DTVNFDVAGR YLYGAPAAGN SLQGQLFLRP MREAVAKLPG
FQFGDINEQN LSRSLDAVEL TLDEQGHTTV SAESQWGDVH SPLRLILQAS LLESGGRPVT
RRVEQAIWPA QAMPGIRPQF ASKEVYDYRT DTTRTQPIVD EDSSAGFDIV YADAQGEKLA
VNDLDVRLIR ERRDYYWSWE ESEGWQSQYD QKDLVEAEQK LTLAAGETGK VAFPVEWGSY
RLEVRDPENN LVSSLRFWAG YSWQDNSDGT GAVRPDRVTL KIDKPSYKAG DTINLHIAAP
AAGKGYALVE SSDGPLWWKE IDVPAGGIDL AIPVDKSWQR HDLYLSTVVI RPGDKARSAT
PKRAVGILHL PLGDESRRLD LTLQNPAKMR PNQNLTVKVK ASVKNGEVPK QINVLLSAVD
SGVLSITDYK TPDPWDAFFG RKRYGADIYD IYGQVIEGEG RLAALRFGGD GDEGDELSRG
GKKPVNHVTI IAQQAQPVAL DENGEGTVTL PIGDFNGELR VMAQAWTDDR FGNSEEKVTV
AAPLVSELAA PRFMASGDTS RLALDLTNLT DRPQQLSVAL SAQGLLALNG ASTMDVKLAP
GARGTLFIPV RALAGFGDGE IKAVINGLAL PGETLADPVK QWKIGVRPAF PAQTVNSGAV
VKPGETWTLP PAHLSGIAES TLEGQLLLSG RPPLNLARYI RELKAYPYGC LEQTTSGLFP
SLYTNESELN ALGIKGITDQ QRRGAIDVGI ARLLEMQSDN GGFGLWDKSG PEEYWLTAYV
TDFLVRAGEQ GYSVNGDALG KANQRLLRYL QDPGLIALRY SDDAPASRFA VQAYAALVLA
RQQKAPLGAL RELWQRHEQA RAGLPLVQLG IALKLMGDEP RSQQAIALGL KTQRSDKQIW
MADYGSELRD KAMMLSLLEE NKLLPDSQNQ LLLELSDMAW SQRWLSTQET NALFIAGHGL
QNVKGDWQAQ TSLGAEPLAS SQAVTRNLTA QQLSGLQVTN TGMASLYLRL DSAGYPQQAP
AAYSNVLHIE RHFLDAKGNT RSLASLKSGE LVMVWLDVWA DKNVPDALVV DLLPAGLELE
NQNLANSSAS LGDSASEVQT LLNQMQQQDI QHMEFRDDRF VAALPLNEGQ HATLIYLARA
VTPGSYSVPV PQVESMLRSR RGYLWLIAPL LVAAFVWLAD KLWPLPLREV NPARVVVAAD
GTPLWRFADA EGIWRYSVTL NQVSPRYLEA LIGYEDRWFW DHPGVNPFSI LRAAWQDLRS
GEVISGGSTL TMQVARLLDP HPRTLGGKVR QVWRAFQLEW HLSKAEILTL YLNRAPFGGT
LQGIGAASWA YLGKSPEQLS YSEAAMLAVL PQAPSRLRPD RWPDRAQLAR DKVLRRMAEQ
GVWPRQQVNE ALQEAVWLAP RQMPQLAPLL SRALVAKSKA TLIATTLNAP LQRQLEELAL
NWKSRLPPRS SLAMLVVDHT TMQVRAWVGS ADINDDSRFG HVDMVTAIRS PGSVLKPFVY
GMAMDEGLIH PASLLQDVPR RFGDYRPGNF DTGFHGPVSM GDALVRSLNL PAVQVLEAYG
PKRFAGQMGN VGLNLRFPQG SEPNLSLILG GGGARLDQIV AAYSAFARHG KAAQLRVLAS
DALRERPLMS PGAAWIIRRI LAGEAQPQPD ETLPPVVPLA WKTGTSYGYR DAWAIGINSR
YLIGIWTGRP DSTPVAGQFG LGSAVPLLNQ VNNLLQANSR VQQLHLPTDP RPASVTAAEV
CWPGGQALSA GDVNCRRRLA TWLLDDAQPP TLLAPGQEGS QGTRQLIWVD AQGKRVAADC
PGARQQTVAL WPLPLEPWLP QAERRAARLP AVSESCPPLQ KESVTPLLLL GVRDGTILKR
LPGQMQLPLR LSSQGGQGQR WWFINGESEE STGDGLALML GKPGDYQVLV MDEFGQVASA
NFTLQ
//
