ID A0A094P7F1_9ACTN Unreviewed; 688 AA.
AC A0A094P7F1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cell division protein FtsI {ECO:0008006|Google:ProtNLM};
GN ORFNames=GM46_9765 {ECO:0000313|EMBL:KGA06827.1};
OS actinobacterium acAcidi.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA06827.1, ECO:0000313|Proteomes:UP000029305};
RN [1] {ECO:0000313|EMBL:KGA06827.1, ECO:0000313|Proteomes:UP000029305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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:KGA06827.1}.
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DR EMBL; JNSG01000096; KGA06827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094P7F1; -.
DR PATRIC; fig|1504320.4.peg.1964; -.
DR Proteomes; UP000029305; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 161..308
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 352..660
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 72506 MW; D7B191AE68120C20 CRC64;
MSRAEGIQRG SRSHGSPSQR SSSAHRSRSQ TSQRASTRPG ESRTRPTSSG TSAASRRSAT
HQSSRTVRQQ PTAPSPFQSR AIELWIALKV FISGEIPAGL KEGKVTSAAA HQAVKRRLGV
AFVLLTSLLL IAAARVVLVQ TKMRGDYLVA SLDQRTRIST VRAARGVIFD RNGNELALSI
PSRTVFADPR DIEDFPGTAR TLAVALGYTP EQEAKLLTDL SVPGEKFHYI ARQLDEPAAQ
AILGLGLKGV YSYTEPARQV EGGVAAAIIG RTDPDGVGTS GLEKQFNKSL TGLDGQLQRE
VSKTGGAIAG SNQTIVAPVP GDDIVLTIDK NIQFQTDSAL IERVGRLSAK GGTAIVMNSR
TGEIYAMSNV RRDASGAVVT ATGNFAAVEA YEPGSVAKVF SVSAALNEGT VNADTMLKVP
GVVTVDKFPI RDAWPHGVID MSVRSIVSES SNIGTMLTAQ TIKTSTLHDY LSAFGFGKKT
GLNYPGESRG ILRDADKWRG TEKVTVSYGY GLAVTPLQMI AGVNTVANNG TYIAPKLVSA
TIDKSGLRRE VKGSTTRKVL KPETAATMQS MLRDVVCTGT GEQAQVKGME IAGKTGTGYK
VQSNGTYQTD SGGRKYFASF AGFFPASSPE VTILVSIDEP DAQSRDRFGG TAAAPVFARL
VPAVMHELGI EATGAGTGCK AGAAPAGH
//
