ID F2RI49_STRVP Unreviewed; 589 AA.
AC F2RI49;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Cell division protein FtsI {ECO:0000313|EMBL:CCA55032.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:CCA55032.1};
DE Flags: Fragment;
GN OrderedLocusNames=SVEN_1745 {ECO:0000313|EMBL:CCA55032.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA55032.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA55032.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; FR845719; CCA55032.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RI49; -.
DR STRING; 953739.SVEN_1745; -.
DR KEGG; sve:SVEN_1745; -.
DR PATRIC; fig|953739.5.peg.3854; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_5_11; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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:CCA55032.1};
KW Cell division {ECO:0000313|EMBL:CCA55032.1};
KW Glycosyltransferase {ECO:0000313|EMBL:CCA55032.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Transferase {ECO:0000313|EMBL:CCA55032.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 34..202
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 248..563
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCA55032.1"
SQ SEQUENCE 589 AA; 62419 MW; 913834ADDA9935A5 CRC64;
VMLAFVVRLL QVQAVDASAY AAKADKYRFQ EYTLSAERGE ITDRNGIALA ASVDAYDITA
DPKLFTPEEA KVPDAPEQAA ALLAPLLGKE PAELAKKLRT PKSRYTLLAR KQTPQVWNQI
KDLRRVYGQK AQPSAGGNGV NLLGGILSEP STKRVYPNGE LAAGILGYVN AEGKGAGGVE
SMLDGELAGQ DGKIRFTQSG GRQVPTAGSQ GTPAVPGSDI ELTIDRDIQW AAQQAITEQV
TKSKADRGYV VVQNTRTGEV LAMANAPGFD PNDLSAANAA AMGNAALQDA YEPGSTSKVM
SMAAVLEEGK ATPDTHVTVP NRLHRGDRLF KDDVDHETWY LTLNGVLAKS SNIGTILATG
QLGATQAESN KVLHSYLRKF GMGSPTGLDY PGETPGILAK PEDWSTSQQY TIPFGQGLSV
SAMQAASVYS TIANGGVRVE PTLVRGTKGP DGRFTPAAKP QESRVVSEKT AKTLAQMLES
VVDDREGTGN KAAIPGYRVA GKTGTANRVD PELGRYKGYT ASFAGFAPAD DPQITVYCAI
QNPTKGSYFG GQLCGPIYKK VMEFALKTLH VAPTGSQPAR LPVTFEPTP
//
