ID A0A292Z2R4_9PSEU Unreviewed; 616 AA.
AC A0A292Z2R4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Cell division protein FtsI {ECO:0000313|EMBL:GAY10644.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:GAY10644.1};
GN ORFNames=TOK_5005 {ECO:0000313|EMBL:GAY10644.1};
OS Pseudonocardia sp. N23.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY10644.1, ECO:0000313|Proteomes:UP000222857};
RN [1] {ECO:0000313|EMBL:GAY10644.1, ECO:0000313|Proteomes:UP000222857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N23 {ECO:0000313|EMBL:GAY10644.1,
RC ECO:0000313|Proteomes:UP000222857};
RA Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4-
RT dioxane-degrading ability.";
RL Submitted (AUG-2017) 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:GAY10644.1}.
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DR EMBL; BEGX01000057; GAY10644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292Z2R4; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000222857; Unassembled WGS sequence.
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:GAY10644.1};
KW Cell division {ECO:0000313|EMBL:GAY10644.1};
KW Glycosyltransferase {ECO:0000313|EMBL:GAY10644.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transferase {ECO:0000313|EMBL:GAY10644.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 82..232
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 284..592
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 63708 MW; 5119ADE628E65E1D CRC64;
MPVAPPRSRP AGPARTAPPR RPVPPRPAPT RSGDPSRRMK IGRLVLVALL TLSLVKLISV
QTVQSGSLTA SSEKQRLTRF PLPAERGSIL DRNGTPLAFS TEASALVTNP RLITQQKGAQ
AAAYKQQIAT AVAARTGGDP NALLASLNSD KGYVVLAPLA DPGAARELRA AFPEIAEEKR
ESRQYPGGSL AANVIGAASW NSGDQKLTGL VGLESSQDAL LAGTDGYEVV DTAEGSSAII
PGSTRAQQDA VPGSDIQLTI DSDMQYTIQR QLQDYVAKTN AKGGSAVVLD VKTGEVLALA
NGTTFDPSNL AGSDPAAMGN AAVTSPFEPG SVNKIVTMSA ALEYGVAKPD DVLDVPGSIK
VADRTVNDAW KHGLDHYTLT GVLAKSSNVG TIMTAQKVGE DRFADMLARF GLGQKTGIGL
PGESAGKVPA RDTWSGSTFG NLPIGQGLSM TVLQMAGMYQ AVANDGVRIP PRIVASTVGP
TGVRTAPPPP EPVRVVSPQT AQTLRGMLTA VTQNAKGVQR GTGAAAGVDG YQVAGKTGTA
QQVDPSCGCY ARSTYWITFA GMLPAQDPRF VIGIMLDAPA GGASAAPLFH DMASYIAARQ
QIPVGPPAPF QTLVAP
//
