ID A0A0T5ZQS7_9BACT Unreviewed; 599 AA.
AC A0A0T5ZQS7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidoglycan transpeptidase, penicillin-binding protein 2 {ECO:0000313|EMBL:KRT65180.1};
GN Name=mrdA {ECO:0000313|EMBL:KRT65180.1};
GN ORFNames=XU11_C0033G0010 {ECO:0000313|EMBL:KRT65180.1};
OS Candidatus Dadabacteria bacterium CSP1-2.
OC Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT65180.1, ECO:0000313|Proteomes:UP000051780};
RN [1] {ECO:0000313|EMBL:KRT65180.1, ECO:0000313|Proteomes:UP000051780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT65180.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT65180.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDXN01000033; KRT65180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZQS7; -.
DR STRING; 1640508.XU11_C0033G0010; -.
DR PATRIC; fig|1640508.3.peg.1808; -.
DR Proteomes; UP000051780; 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 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..218
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 258..588
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 599 AA; 66312 MW; DEE358B2F5A6833E CRC64;
MREYKRRFLL VTIIIANAFL ILVGRLWYLQ IVRGEEFEKF SLDNRVRSIR IPAPRGRILD
RRGREIVVNR PSFDIYILPE DIQNPDTLSS LLSPILGIEP NTIRSKIKTA LQKSRFKPAL
LAKDINRDQL AFIEARKSSL PGVLVEVNHI RRYNQGTLGA AFLGYMGKIN EDELKLYPDV
RVDDVVGKSG IEKGWEVYLH GKDGYIQKLT DAFGREVKWS LFKEDLHRQD SVPGSDVVLS
IDLDLQYAAE EALGDRRGAV VAVNVNSGEI LALVSHPTFD PSDFIKGIDA AKWKYLLEDK
SSPLTNRATQ GVYPPGSVFK IVTAVAGLAE GVINSDTYFY CPGRYKFGKK TFKCWKGGGH
GSLNLHQAIV ESCDVYFYNV AERLGIDRLS RYIKRFGFGT PTGIELNEKV GISPSREWKV
KTLKKPWYEG ETIVTAIGQG YLSATPLQIA IMTSAVANGE KLIKPRVVRE VISPDGKTLA
RYNRQETGNI GIEGTIINII KDALEGVVNE PNGTGRAARL DEMVVAGKTG TAQVVSSSVS
TNQEDYKDHA WFTSYAPAGN PEIAVTVLVE HGGKGGAVAA PIVKQILEAY LKLKKEGSV
//
