ID   F2R3Q9_STRVP            Unreviewed;       491 AA.
AC   F2R3Q9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Cell division protein FtsI {ECO:0000313|EMBL:CCA58281.1};
DE            EC=2.4.1.129 {ECO:0000313|EMBL:CCA58281.1};
GN   OrderedLocusNames=SVEN_4995 {ECO:0000313|EMBL:CCA58281.1};
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:CCA58281.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA58281.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA58281.1};
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}.
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; FR845719; CCA58281.1; -; Genomic_DNA.
DR   RefSeq; WP_015036180.1; NZ_JABVZO010000457.1.
DR   AlphaFoldDB; F2R3Q9; -.
DR   STRING; 953739.SVEN_4995; -.
DR   GeneID; 69867063; -.
DR   KEGG; sve:SVEN_4995; -.
DR   PATRIC; fig|953739.5.peg.129; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_0_11; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000006854; Chromosome.
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; 3.40.710.10; 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; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:CCA58281.1};
KW   Cell division {ECO:0000313|EMBL:CCA58281.1};
KW   Glycosyltransferase {ECO:0000313|EMBL:CCA58281.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:CCA58281.1}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..491
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038374623"
FT   DOMAIN          155..480
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   491 AA;  51913 MW;  90978368A445B062 CRC64;
     MIRYARRAAA LCLVLLVALL VNSARVMVFE AESLDDNPAN RRIAINRYAQ PRGEIVVDGK
     PVTGSRDSGQ QLRWERTYRQ GPLYAPLTGY SSQTYGTTLV EHAEDDVLSG TEPMLAPLPL
     WNDLTRGRQP GGDVVTTIRA SMQEAAFRGL DGKRGAVVAV EPHSGRILAL VSSPSYDPGV
     LSGTGPGVKE AWRRLNTSPN QPMLNRALRQ TYPPGSTFKI VTAAAALDAG VVRDVEAPTD
     TPDPFVLPGT RQVLPNEATG CGDASLAYAI QWSCNTVMAG LGVEVGLAGM VDAVERFGFN
     DTALRVPSWV AKSNFDREMS PDQLALSSIG QFDTTATPLQ MAMVASAVAN NGEIAQPYLV
     DRTTTSGGTT VDRTGRRSYR QAMNPATAMQ LQRLMLKAVA DGTGTNAAIP GARVGGKTGT
     AQHGFGNTGT PYAWFIAWAQ AEDSAQPAVA VAVVVEDAEA ARTDISGGGS AAPIAKAVME
     EALRLEAKAR G
//