ID A0A0B1ZZQ7_9MICO Unreviewed; 876 AA.
AC A0A0B1ZZQ7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=PASTA domain-containing protein {ECO:0000259|PROSITE:PS51178};
GN ORFNames=LK09_14190 {ECO:0000313|EMBL:KHK96705.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK96705.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK96705.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK96705.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-2014) 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:KHK96705.1}.
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DR EMBL; JTDK01000013; KHK96705.1; -; Genomic_DNA.
DR RefSeq; WP_039400760.1; NZ_JTDK01000013.1.
DR AlphaFoldDB; A0A0B1ZZQ7; -.
DR STRING; 1348253.LK09_14190; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000031030; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000031030};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 766..831
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 807..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 91682 MW; 02DC4AB0E9030DFF CRC64;
MSQKRTVAGV LGGLFGLVGL SVLAGILVTV LVTPAVTVTS SAATRAITLF EDLPSALTID
KISLPSTLYY QNPTTHQEVV LAKFYDQNRS PVKWGQIAPV MYDAILSSED KRFYEHGGVD
PVGTTSALIS NITGRSSRGG SSISQQYVKN VLIQQCDWNA TGNSVDAANR CWQQAAGVTG
TAGIQRKIQE MRYAIALEQK YSKNEILLGY LNIALFGGTT YGINAAAKYY FGVPASKLTL
ARAAILAGMV QNPNTYRIDL PGGTATVNGK AVNGKNDKIA LVQVGDHYDM VDPASAPKDA
VKITGYSLTK QRELYVLGQM LKDGKITQKQ YNDAAIAPIV PKITQPSFGC AYSVAPYYCQ
YVRNTILADK AFGATATDRG RMLQKGGLKV YTTLDPRVQK AAQDAQDAYV PTHVSYMRLG
STSVSLQSTT GRVLAIAQNT KYSDTSNKDG YQTVIYAGDA KNGASGGFNA GSTFKLFTLL
TWLKDGHPLN EIVNGNHQSF FRWHDSCLPR GRLIEPTGYQ PGNFQHEAGR FGTPLEFTKI
SLNSGFWAMA HELDLCEIGK TAASLGVTLG DGAPIPLSTS GGKSSPGGYP SPYEVLGSDN
VSPLAMAAAY ATIANKGIHC QPKVIDRVTD AGGTPLPIPK TTCTQVIAPK IAATAAYALK
GPMSPGGTGA LGNPNDGTEL IGKTGTHQSF ETWLDTSSTA VTTANWVGAW GGISSDTNSA
PRMDLHYYRG TLLWNIRYAL AHDIQGAIDK WYPGGSFPPP DPKLTGVGQK SVPNVVGMSV
GDAIQALLKA GFGWVISAPV SSGLPAGTIA QQDPAPGVTS AGRRVTISPS DGSGAASGGG
GNGNGSGNGG NSSPSPSPSP SGTGDGHGHG HGGGHG
//
