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Database: UniProt
Entry: A0A1G6KHN6_9PSEU
LinkDB: A0A1G6KHN6_9PSEU
Original site: A0A1G6KHN6_9PSEU 
ID   A0A1G6KHN6_9PSEU        Unreviewed;       613 AA.
AC   A0A1G6KHN6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Cell division protein FtsI (Penicillin-binding protein 3) {ECO:0000313|EMBL:SDC29816.1};
GN   ORFNames=SAMN05216174_101888 {ECO:0000313|EMBL:SDC29816.1};
OS   Actinokineospora iranica.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=1271860 {ECO:0000313|EMBL:SDC29816.1, ECO:0000313|Proteomes:UP000199501};
RN   [1] {ECO:0000313|Proteomes:UP000199501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10403 {ECO:0000313|Proteomes:UP000199501};
RA   Varghese N., Submissions S.;
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; FMZZ01000001; SDC29816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6KHN6; -.
DR   STRING; 1271860.SAMN05216174_101888; -.
DR   Proteomes; UP000199501; 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:SDC29816.1};
KW   Cell division {ECO:0000313|EMBL:SDC29816.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199501};
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..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          56..226
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          277..588
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          474..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  66334 MW;  F79DD710D8166A06 CRC64;
     MTKRAAGTDH RVRVVVVRFL LIASLVAAGL KLVQVQGFEA EALASRAERQ RVQKIPIPAT
     RGSILDRNGV ELAFSVEARA LAFQPNLQRK QIAEFNRKHP DKQVSFDEET AAIARRMREL
     LGPQLSEEDL LAKLRSDDAF VYLTTTAEPA AARRLKEEFP QLNVEYRAVR EYPGGTLAAN
     VVGFANWRME DKDHQKHNLH GLVGLEMLRD NDLSGTPGSQ MVETEEGADV IIPGTERDLQ
     PAVDGKDIEL TIDADLQFFV QQKAAEYAQR SGAKSASVVV MDAKTGEVYA LANDKTFDPS
     TRGGRDPNLM SDPAVTTPFE PGSVNKVVTA MAALEYGVTT PDAVHAVPGS IKVADRVVGD
     AWDHGTLNMT TTGVFAKSSN VGTLMIANQV RPERFADMLG KLGIGKRTGI GLPGESPGKV
     LPQSQWSGST YGNLPIGQGL SMTVLQMAGM YQTLANDGVR VPPRIVKAKI APDGTRLDEP
     RPEPVRVVSP ETARKTRDML RAVTQKAPNQ NSGTAPAAAL TGYQISGKTG TAQQFDQAAG
     RYSNSKYWIT FAGILPADNP RFVIGMVYDT PAYSTPDGHS AAPFFHDVAS FIAQRYNLPL
     SKEPTPVVPL VVP
//
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