ID A0A2U1FD07_9PSEU Unreviewed; 1005 AA.
AC A0A2U1FD07;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Cell division protein FtsI/penicillin-binding protein 2 {ECO:0000313|EMBL:PVZ10048.1};
GN ORFNames=C8D89_105124 {ECO:0000313|EMBL:PVZ10048.1};
OS Actinomycetospora cinnamomea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinomycetospora.
OX NCBI_TaxID=663609 {ECO:0000313|EMBL:PVZ10048.1, ECO:0000313|Proteomes:UP000245639};
RN [1] {ECO:0000313|EMBL:PVZ10048.1, ECO:0000313|Proteomes:UP000245639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45771 {ECO:0000313|EMBL:PVZ10048.1,
RC ECO:0000313|Proteomes:UP000245639};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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:PVZ10048.1}.
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DR EMBL; QEKW01000005; PVZ10048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1FD07; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000245639; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; IPR001182; FtsW/RodA.
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:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 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:PVZ10048.1};
KW Cell division {ECO:0000313|EMBL:PVZ10048.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245639};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 562..639
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 682..997
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 102550 MW; E4FAD9B25965771A CRC64;
MLSGGSTDGW DEPAPRGPAP GDGWDRDRRR PGVRLRRALR RLTHRPGRPS RADRAEQRRA
RARARDERGL EPPRAAWGDI LALLAAVVLV VLGAANLAAM GDVGATTTKL ATGGLGLALL
FLLAARRIAV TPALAWTVYG TTLALLLAVL VVGREVNGAL RWLAVGGITL QPSELAKIAV
PLVLAAVLTR GRPTWRRFAV ALPLAAVPIV LVADQPDLST ATLLTLTTAA VLVIARVPTR
YLLPVLAAAV VAAPLAVGLL RDYQAARLGT FLTGSQSAEG PGWAVRQARL AIARGGWWGD
RTDPVHLLAA RYLPERQTDL ALASLASGWG AVAAALALLA GLVIVWRCVL GARAPRSATG
RLLCAGFAVL LAVELVVSTG GNLGLLPVAG VPFPILSGGG TATVVHLAAL GLALSARRDG
ARRQLWTPAA RSSPRLARTT VAALTVVLVA FASFGAGVVR DPVAAAASVD QMTRCVTIPA
PRGAVVDRHG ALLAADAGDR GIRVAPALLR RDPAAVDRLA ALLGRPPGEL HALVDPAPDT
VVGLDAGTVP GPVGETVARA GLPGVVVVPA PRRSYPTGPV LAPVLGWVGL ATPRQTALHP
DLDPRGTTGR AGVEQSYDAV LRGVPGEQCY WVDPVGRPMS AAARRDPVPG ATLALTIDLG
MQQRLVADVA ASLSGSARGA VGGAVAMDPR TGAVLAMASW PSHDNALYGP PLDTAALRAT
SRAPGTPMIN HAIGSALPPG STFKLVNATA NMITSTIPPE RVLPGGGSFT YGGHSFGNWR
VLPAQNLVDA LAWSNDVYFY QLALALGPET MIDTARALGV GSPTGIDLPG ESAGYLGTPA
SVEAAGGTWY PGTTVILGIG QGPLQVTPLQ SARWTAAVAT GALPTPYVGM AVGTGPGAIA
LPHPAPTPLP FADRLGPVRE GMRAVVTSGT GRALADVGVP VAAKSGTAED PSVPGGGVDD
WMTAVAPADS PDLVVTALAQ RPETGTSRTA AVVAATMRAH GAGAP
//
