ID A0A117PM15_9ACTN Unreviewed; 654 AA.
AC A0A117PM15;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Cell division protein {ECO:0000313|EMBL:KUM82089.1};
GN ORFNames=AQI70_01925 {ECO:0000313|EMBL:KUM82089.1};
OS Streptomyces curacoi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM82089.1, ECO:0000313|Proteomes:UP000054024};
RN [1] {ECO:0000313|EMBL:KUM82089.1, ECO:0000313|Proteomes:UP000054024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM82089.1,
RC ECO:0000313|Proteomes:UP000054024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT the species Streptomyces curacoi.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:KUM82089.1}.
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; LMWJ01000001; KUM82089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117PM15; -.
DR STRING; 146536.AQI70_01925; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000054024; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.330; -; 1.
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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:KUM82089.1};
KW Cell division {ECO:0000313|EMBL:KUM82089.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000054024};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 103..273
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 316..631
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 69736 MW; AD439F3877BC16FA CRC64;
MTEVSDREPP RRRVPGPAKP ARSGGAQRRQ GPGARPARRP APPRPAARII RLGSPRPRLR
MVGLALTLVL SAFVVRLLQV QAVDASTYAA KAEKNRYVGY TLAAERGGIT DRNGVALATS
VDAYDITADP TLFSREQLKI DDGPEQAAAL LAPILGQEQE TIVRKLRPEN KNSRYTLLAR
RQTPQVWKQI KDLKNALATK AEKDKSTVNV LAGVLSVASS KRVYPNGDLA AGILGWVNAD
GKGGGGIEQQ LNKELSGKDG EIRYAQSGGR QVPTVSATET PAVPGSDVEL TIDRDIQWAA
QNAISEQVKK SRADRGYVIV QDARTGQVLA MANSPGFDPN DLAEASGENM GNAAVQDAFE
PGSTAKVMSM AAVLEEGVAT PGTHVVVPNR LHRGDRLFKD DIDHETWYLT LNGVLAKSSN
IGTILATGQL GRTQPQANRV LYDYLRKFGL GSYTGLGFPG ETPGILAAPD KWSTSQQYTI
PFGQGVSINA MQAASVYSTI ANGGVRVEPS LVRGTKGPDG QFTPAPAPKK TRVISAKTAK
TLAQMLESVV DDREGTGTKA RIPGYRVAGK TGTANRVDPA TGKYRGYTSS FAGFAPADKP
RVTVYCAIQN ATAGNYFGGQ ICGPIYKQVM EFALKTLQIP PTGARPAKLP VAYN
//
