ID A0A1G2HHB8_9BACT Unreviewed; 648 AA.
AC A0A1G2HHB8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:OGZ61892.1};
GN ORFNames=A2932_00400 {ECO:0000313|EMBL:OGZ61892.1};
OS Candidatus Spechtbacteria bacterium RIFCSPLOWO2_01_FULL_46_10.
OC Bacteria; Candidatus Spechtbacteria.
OX NCBI_TaxID=1802163 {ECO:0000313|EMBL:OGZ61892.1, ECO:0000313|Proteomes:UP000179153};
RN [1] {ECO:0000313|EMBL:OGZ61892.1, ECO:0000313|Proteomes:UP000179153}
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:OGZ61892.1}.
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DR EMBL; MHOI01000007; OGZ61892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2HHB8; -.
DR STRING; 1802163.A2932_00400; -.
DR Proteomes; UP000179153; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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 64..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..277
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 318..642
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 648 AA; 71233 MW; 7837AAD55E85100D CRC64;
MFAFIKKLFN GNRGLHIDLE TLRDIAPEDI LPDFGFEKSS GEAPMLQGDE YNQKKLEIPV
RAKSVHLTFF LFFALIAGIL GYTLFLFVAR GDEYSSIAAN NAMQIYEIGP SRGDIISADG
VVIASSTVVF DLVVAPSKLT TQEAENLAAD ISKLFNDTSQ DELFQQIRAA QSRNLGEQIL
IKSISQDDAG GLTSVLDKYD FLQLQQRSVR SYPYNSLYAH IIGYTALVSA EDLENFSDYD
LNDQIGKKGI EFYFEDDLKG RDGLFAKIIS SQGAITGERL VREIERGSDI QLTINHDLQL
KSREALLNAL EEYQIKSGAV VALNPKNGDI LAFVSLPDFD PNDFTRGLSQ KDFQSYFENS
VQPLFNRVTQ GEYASGSVIK LIIATAALEE NVISPNQYIL THGYIDVPSV YDPNVTYRFY
DWKDHGAVNM REAIAVSSNV YFYTIGGGFD GQEGLGIERI SDYLKRFNWG RTFGLDFGTE
SAGLVPTPQW KQAVKNENWT IGDTYNVSIG QGDILATPLQ VASATAVFAN GGTLWRPDVI
ASVGGKDAGP LQAISRNLLS DDSLGVVRSG MREAVLSGSS RYLSTLPSAV AGKTGTVQAS
GGDNHAWFTG FAPYENPEIV VTVLLERGRD STNAVRVAHE ILNWYLAK
//
