ID   A0A0G1L0K0_9BACT        Unreviewed;       618 AA.
AC   A0A0G1L0K0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KKT89283.1};
GN   ORFNames=UW89_C0001G0011 {ECO:0000313|EMBL:KKT89283.1};
OS   Parcubacteria group bacterium GW2011_GWB1_45_10.
OC   Bacteria.
OX   NCBI_TaxID=1618877 {ECO:0000313|EMBL:KKT89283.1, ECO:0000313|Proteomes:UP000033817};
RN   [1] {ECO:0000313|EMBL:KKT89283.1, ECO:0000313|Proteomes:UP000033817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT89283.1}.
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DR   EMBL; LCKC01000001; KKT89283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1L0K0; -.
DR   STRING; 1618877.UW89_C0001G0011; -.
DR   Proteomes; UP000033817; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR017790; Penicillin-binding_protein_2.
DR   NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..244
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          284..608
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   618 AA;  69694 MW;  67A7A49156C1DF51 CRC64;
     MKLKRNNSFI IEPEEILLEN NAVFAKRLEF SIGRKYVFFI LGLVAFFMFL SLGVAFKLQI
     FQHPAYARRS EENSLRNIFL EAPRGLIFDR YGDVLADNQV YFEVLPIKEN LDSGHNFELQ
     LETLSRISGI AKDEISQKLD SNKEVVFENF DLDKAIEFKA NEALMPGFKL VGRYQRHYPL
     KEATSHVLGY TGLVTEKEHA ENQDLSLSQT IGKVGVELFY DSYLRGSRGS FSYQVDVKDD
     LIGQEKSNYF KTGNSIRLTL DAKLQEKIYQ IFRDNVFDAG SGAVAVALEP KTGEILALVS
     YPGFDTSKKI WSDSKAQPFF NRAVSGEYSP GSTIKPFIAL AALEEKIIDP LFKVDDTEGK
     ITIENPYFPD QPYIFRDWKA HGFVNMEEAI ADSANVYFYT IGGGYGNIKG LGVERIKEYL
     EKYGWGKKTE TDFLGEKPGF LPDPEWKEKT FKDIWRIGDT YHYSIGQGYV KTTPIQLAAN
     YQLFANLGKV FRPFLINSVF NSEGGQEVYH GSPKVLREYQ IDENYFKIVN RGMERTVIDG
     SAAGRMAGLP FSVAGKTGSI QTSSSLTDTN AAFVSFIPAE DPKFLLLVLV ESGGSGGATA
     VPLAKQILYW YWENRISE
//