ID A0A1G2CH13_9BACT Unreviewed; 625 AA.
AC A0A1G2CH13;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:OGY99940.1};
GN ORFNames=A3B13_02010 {ECO:0000313|EMBL:OGY99940.1};
OS Candidatus Liptonbacteria bacterium RIFCSPLOWO2_01_FULL_45_15.
OC Bacteria; Candidatus Liptonbacteria.
OX NCBI_TaxID=1798649 {ECO:0000313|EMBL:OGY99940.1, ECO:0000313|Proteomes:UP000176287};
RN [1] {ECO:0000313|EMBL:OGY99940.1, ECO:0000313|Proteomes:UP000176287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY99940.1}.
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DR EMBL; MHKZ01000032; OGY99940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2CH13; -.
DR STRING; 1798649.A3B13_02010; -.
DR Proteomes; UP000176287; 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 38..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..248
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 293..613
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 625 AA; 69927 MW; 73C60AEB2E9D635A CRC64;
MFFRRRKKEL NLEETLSDDW AKDKDAELVE VPLGNWPMVL AGLCVSFITI VLAGRIAFVG
LAQSTRYELR AEDNQNLVSF LPAPRGIIYD RNGKIIADNK PVFSAYLKTD EFLRQTDSQE
QVLDYIGGIL SLSREEIWNS LKSSDLERNN GLLLLNPDLS QEEAVKLKSL NLRSVEIADN
FDRNYPNGEI FSSILGYTGM VTVSDLKNNS NLMIHDEIGK GGVELYYDDE LRGTNGKTIR
KRDARGILLG DKEEIKPEIG KPLYLTIDAD LQRYFYQRMK IQLSSLGRTK GVGLAMNPQN
GEILAMLNFP VYDNNILSSA GRNPEKQAIL TSRDQPLFNR AIAGFYTPGS TIKPLVATAA
LKEGVITPSK EIFSPGYIDI PNPYKPDEPT RYLDWRYQGY VNLASAIAQS SNVYFYEIGG
GGPDSAGLGI TRLRQWWQKF NLGNLTGIDL PGEAKGFLPS PEWKEKKDKQ PWLLGDTYNV
SIGQGDLLLT PIQLIEYISA IANGGKVFQP TVNKNVEHKI ISDLSYLNQQ FQEVREGMRL
VATSKLSMAN TLGELPFAVE GKTGTAQVRS NQQQNAFFVG YATSENPQIA VLVLVENSRE
GSLNAVPIAK DIFNWYYENR IKNSK
//
