ID   FTSIH_NEPOL             Reviewed;         709 AA.
AC   Q9TL36;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase FtsI homolog {ECO:0000305};
DE            EC=3.4.16.4 {ECO:0000250|UniProtKB:P0AD68};
GN   Name=ftsI;
OS   Nephroselmis olivacea (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC   Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX   NCBI_TaxID=31312;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-484 / S-N-5-8;
RX   PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT   olivacea: insights into the architecture of ancestral chloroplast
RT   genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000250|UniProtKB:P0AD68};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: The presence of this gene in the chloroplast genome
CC       suggests there may be an unsuspected vestigal peptidoglycan layer in
CC       this organism's chloroplasts.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR   EMBL; AF137379; AAD54780.1; -; Genomic_DNA.
DR   RefSeq; NP_050809.1; NC_000927.1.
DR   AlphaFoldDB; Q9TL36; -.
DR   SMR; Q9TL36; -.
DR   GeneID; 802005; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 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   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 2.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Cell shape; Chloroplast; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Plastid; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..709
FT                   /note="Peptidoglycan D,D-transpeptidase FtsI homolog"
FT                   /id="PRO_0000195462"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        341
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD68"
SQ   SEQUENCE   709 AA;  79946 MW;  FE8782C9D20A5AC4 CRC64;
     MIYNYPMKYR RQFRRLPKHL QGIYYAFLSI STMIKIALDP YSKRPMKWMH SGTPFQYENE
     RMVMIKLSLA TVGLLFATRL SGLQFNKYTE LKSVAERQQI GQVNDPQQRK IILDHHGDIV
     AIDLPAYDLY VHPRMCSISL ERIAELLSPI LDLSSQYLYN RLDEGDSGIC LMHQIDTNTS
     AQIRRLGVDG IELVHHPQRV YPKRGSFESI LGYVDTEGYG QAGLESSLDD WMKSTYQDVP
     CWMDGHGNFL GIRFPKQILF HQESALQLTI DCGLQEKVSQ LITNAMNRFG AKRIAAIIME
     AHSGAIRCLA TSPSYDPNCY GWFPMERFRC WPITDLFEPG STFKPVNLAI ALENGIFQPT
     DRILDTGKIR IGDSWIGNVG GGFIWDRSLD HLTGTQILQR SSNVGMVRVM QSLDPAIYHR
     NLIRLGLGSH RNDNQTSFKM SSHDHNESGW NLKDLTSDYA ISVVKDQDEF VDHEIEAATA
     SFGQGLAMTP LKLLQLIATI ANGGMAVTPH LISKIVTLDH FHHLQSMNEF SLQGWVGQSV
     LSRSQYHAKQ PRPYTHDLYL GHVPVPSLEL GWFDVKSIPP HTRERRRLFS RQTCNVLLGM
     LEQVVLDAQA TGSRGFLPGY AMAGKTGTAQ KASALGGYST DSVVTSFVGI YPAVKPKFVT
     LVIIDEPEDP FRFGFNTAVD VTQTLISEMI VQEQDPPSYP TVSLFERNM