ID A0A117MDE3_9CHLR Unreviewed; 695 AA.
AC A0A117MDE3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KUK97991.1};
GN ORFNames=XE06_0197 {ECO:0000313|EMBL:KUK97991.1};
OS Anaerolineaceae bacterium 46_22.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae.
OX NCBI_TaxID=1635294 {ECO:0000313|EMBL:KUK97991.1, ECO:0000313|Proteomes:UP000054480};
RN [1] {ECO:0000313|Proteomes:UP000054480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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:KUK97991.1}.
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DR EMBL; LGHA01000011; KUK97991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117MDE3; -.
DR PATRIC; fig|1635294.3.peg.923; -.
DR Proteomes; UP000054480; 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 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..254
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 301..680
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 695 AA; 77198 MW; C31392DC832C27F6 CRC64;
MSVYPQRNSK FENWRFLVLF ILIGTIFGFY ILRLFDIQII QGEDFIAQAN DNRTQVIYEP
AIRGTIYDRN GYILAQNVPS YNVVVTPGYL PADEGDIQDI FRELAELIDM PVSQGDTDEE
TVRNFTPCYN DLGISQIVFI ATTNWPYQST ALKCDVSQDV AMVVMENSED WPGIDIEISS
VRHYPTGELT SEIIGFLGPV PAVLEDYYVD LGFVANRDKV GYAGVEQSLN DILAGRNGRE
LVEVNVAGEI IRTLEEPVEP TPGQDVYLTI DSRLQSIARE ALINELNYWN AYSGRTISNN
GVVIAMNPKT GEVLALVSYP NFENNRMERI IPGYYYEQLS NDPQRPLFNH AISAEHPPGS
VYKMTSALGV LNEGVVTPEY EVEDPGTITV IQRFYENDPG VPRQFVCWDR NGHGMVNFLE
GVAFSCNIYW HKVAGGFGDE VPDGGLGPWL MSEYAQALGY GSETGIELPG ESDGLVPNPT
WKRLTLGENW ATGDTYTAAI GQGFVLATPL QVLNSISTIA NGGKLMDVTI VDKVVDQDGE
IVQQLTPTVR WDITQDPVIN MYDGNVETSE TKTVEPWVIE LANQGMRMVV TEGTASRYET
DRHDDLFRND TSRSAGKTGT AEYCDNVAQA QGLCVPEAWP AHAWYVGYAP WDDAEIAVVA
FIYNGKEGAT FAAPIVRQVI DAYFELKLID TPVQP
//