ID   FTSIH_MESVI             Reviewed;         598 AA.
AC   Q9MUV9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
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   Mesostigma viride (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC   Mesostigmatales; Mesostigmataceae; Mesostigma.
OX   NCBI_TaxID=41882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-296 / KY-14 / CCMP 2046;
RX   PubMed=10688199; DOI=10.1038/35001059;
RA   Lemieux C., Otis C., Turmel M.;
RT   "Ancestral chloroplast genome in Mesostigma viride reveals an early branch
RT   of green plant evolution.";
RL   Nature 403:649-652(2000).
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; AF166114; AAF43792.1; -; Genomic_DNA.
DR   RefSeq; NP_038351.1; NC_002186.1.
DR   AlphaFoldDB; Q9MUV9; -.
DR   SMR; Q9MUV9; -.
DR   GeneID; 800933; -.
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; 1.
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..598
FT                   /note="Peptidoglycan D,D-transpeptidase FtsI homolog"
FT                   /id="PRO_0000195461"
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        291
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD68"
SQ   SEQUENCE   598 AA;  67214 MW;  DB1B7948EB9DB4DA CRC64;
     MNKKKIFGFS RIVLVWILFF SGSSLLLGRL FYLQVMKGSW LTNKAKNQQT IILNTFQPRR
     TICDRNGIPL AIDTLAYDIF AHPLHFKKST FDIANELYSI LNLDVEYLQN LFIKNTTGIC
     IAHQAPEQIA NQIIAKNIEG IELVQHPKRY YPYKQLCADV IGYVNTLHEG QAGLELSCQE
     SLQLQSPEVV SAIDGRGFLI NDGIPRELFK QDSLCLQLTI DLDLQKASYL AIYDGIKKCN
     AKRGTVIILD PYTGAILALV TAPSYDPNVY YDFPIERFKN WPVIDLYEPG STFKPINMAI
     ALEAKAIKKN DFFYDEGCIQ ISDTIITNNN YYNKQFACDK NSHLNITDVL SNSSNVGMVH
     ILQRLAPEIY YQWIQKLGLG NNVFLETDFP LSSYSSLKNI LEFTSYNIES AVTSFGQGLA
     MTPIKLAQLY ACLSNGGNII RPYIVDGLFD IQNEKLFTLN NNIFDQNISL KRKLLKTKVF
     SPSTTEIVLD MLEEVIFNGT GSSCFLPGYR IGGKTGTSQK HAEQGGYSTK HILTSFAAIF
     PINNPQYVIL SVIDEPSIPL SFGSNTAGPV VRSIIESLIR IKKIPPSIPT LTHHYYCK