ID A0A0N7I410_9MICO Unreviewed; 604 AA.
AC A0A0N7I410;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cell division protein FtsI {ECO:0000313|EMBL:ALJ20815.1};
GN ORFNames=AOA12_13245 {ECO:0000313|EMBL:ALJ20815.1};
OS Microbacterium sp. No. 7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ20815.1, ECO:0000313|Proteomes:UP000059097};
RN [1] {ECO:0000313|EMBL:ALJ20815.1, ECO:0000313|Proteomes:UP000059097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ20815.1,
RC ECO:0000313|Proteomes:UP000059097};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a polypropylene glycol-degrading strain
RT Microbacterium sp. No. 7.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP012697; ALJ20815.1; -; Genomic_DNA.
DR RefSeq; WP_054683408.1; NZ_CP012697.1.
DR AlphaFoldDB; A0A0N7I410; -.
DR STRING; 1714373.AOA12_13245; -.
DR KEGG; mio:AOA12_13245; -.
DR PATRIC; fig|1714373.3.peg.2726; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000059097; Chromosome.
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:ALJ20815.1};
KW Cell division {ECO:0000313|EMBL:ALJ20815.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000059097};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..225
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 273..581
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 604 AA; 64796 MW; 29FE0F8B723DD2EB CRC64;
MTTRATRTPR RRTVVALAIV LIVLGAFVVR LIDIQVVNAR EHMTDAREMA TGRAIELHGT
RGDILDATGR VLATSTMLYD VQIDPLLAAK GIQKLDAEGH VVEDADGNDV MVPWPELAAQ
IAAITGQSAD EVRAVVDDAL AADPSSRYGM VARYVPTSTY RALAALELPF LVFPPHPSRT
YPAGAVAGNL LGFVGSDGQP LEGLEEQQNA CLAGADGDLS YQRGADGVII PGTEVETPAE
DGGALQLTID ADLQWYLQQL AEEETARMRA KWGGIMVVEV ATGKIRALAE SGSVDPNDVD
ATEPDNRASR LLRYSFEPGS TYKAITAATV IEQAGLTPTS TVYTPDVMYF DNGARIKDSD
PHPDMNLTLN GALVISSNVA MAQFGELVPP EVRQEYLERF GVGSPDGLDW AGAPQVGFGL
DAADWDAQTY YTTTFGQAFT VTVPQVASTY QIIANDGKKM PLSLVESCVR PDGTVEEPDL
PEPEQVIKAT TAQQVSDMLE NVYSEAWLAD DIAIPGYRVA SKTGTAEVTD GNGGYKQGIY
FTSLVGYAPA DDPQYVVVTV FDEPMTETGS GANRSMFKKA LTQVLTHYRI MPSNSPVPLL
PQTK
//
