ID A0A1I0VKK7_9CELL Unreviewed; 667 AA.
AC A0A1I0VKK7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Cell division protein FtsI (Penicillin-binding protein 3) {ECO:0000313|EMBL:SFA76862.1};
GN ORFNames=SAMN05421867_101455 {ECO:0000313|EMBL:SFA76862.1};
OS Cellulomonas marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=988821 {ECO:0000313|EMBL:SFA76862.1, ECO:0000313|Proteomes:UP000199012};
RN [1] {ECO:0000313|EMBL:SFA76862.1, ECO:0000313|Proteomes:UP000199012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6945 {ECO:0000313|EMBL:SFA76862.1,
RC ECO:0000313|Proteomes:UP000199012};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; FOKA01000001; SFA76862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VKK7; -.
DR STRING; 988821.SAMN05421867_101455; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000199012; 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:SFA76862.1};
KW Cell division {ECO:0000313|EMBL:SFA76862.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199012};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..299
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 343..643
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 67929 MW; D40604CA013AF421 CRC64;
MTTTTPRPAR RAPGATATPG GAARATTTSA TTTSATATRG ATTSTAVRPG VVGTNRRPAS
GAGNARPARA GAGGGGGGAG GRGGRRPGAL GPVAADARGR TAFLTVLVLA LLAVFAGRLV
WVQVVVGPAR AEEALASRLT TRTEVLGTRG QITDADGVAL ATSVERYVVW VNQHQVAEFR
GSDEAPEGAA GVAQLLAPLL DADVAELGGR LVGEAGYKVL QKDVLPEIAR EIRSLGLPGI
GVDMVPDRVY PNGTLAGNVV GFVNSSDQGV AGLEAALDGT LTGEAGWEQY ERGRMGQAIP
GGYSEGDPAR DGLSVRTTIV SDIQWKAQAA LDAQVAATGS DSGTVVVMDP RTGAVLALAD
SGSIDPNSPG GSTGSLTPSV SDVFEPGSTG KVVTMAAALE QGITTPTDQY EVPYTYTTEN
GQTFKDSHEH ELQRLTTTGV LAESSNTGTV MIGQRLSEPT REEYLRRFGF GARTGIELPG
ESAGRLLPAE EWDGRSQYAV LFGQALSVTA VQATSVFATI ANGGVRVAPH LVAGTTDEDG
TFTPAAPAAS TQVVSAETAG TVLSMLESVV DDGTGGSAAI EGYRVAGKTG TAQNWVDGVQ
GITASFIGVA PVDDPRLVVS VILHNPRTSE WGGTVAAPVF QDVTRYALGE LGVAPSGTAP
TLYPTTW
//