ID   FTSA_STRP2              Reviewed;         457 AA.
AC   A0A0H2ZPT5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033};
GN   Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033}; OrderedLocusNames=SPD_1480;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=28941257; DOI=10.1111/mmi.13847;
RA   Zheng J.J., Perez A.J., Tsui H.T., Massidda O., Winkler M.E.;
RT   "Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins suppresses
RT   the requirement for PBP2b by overproduction of FtsA in Streptococcus
RT   pneumoniae D39.";
RL   Mol. Microbiol. 106:793-814(2017).
CC   -!- FUNCTION: Cell division protein that is involved in the assembly of the
CC       Z ring. May serve as a membrane anchor for the Z ring (By similarity).
CC       Increased expression restores growth to a PBP2b (penA) deletion strain
CC       as well as mreCD and rodA deletions, but not gpsB or rodZ deletions.
CC       Does not restore wild-type cell morphology to the penA deletion
CC       (PubMed:28941257). {ECO:0000255|HAMAP-Rule:MF_02033,
CC       ECO:0000269|PubMed:28941257}.
CC   -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_02033}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02033};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02033};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02033}. Note=Localizes to
CC       the Z ring in an FtsZ-dependent manner. Targeted to the membrane
CC       through a conserved C-terminal amphiphatic helix. {ECO:0000255|HAMAP-
CC       Rule:MF_02033}.
CC   -!- INDUCTION: Protein level is negatively regulated by KhpA/KhpB partly at
CC       the post-transcriptional level via its 5'-UTR (at protein level).
CC       {ECO:0000269|PubMed:28941257}.
CC   -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC       Rule:MF_02033}.
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DR   EMBL; CP000410; ABJ55292.1; -; Genomic_DNA.
DR   RefSeq; WP_000090397.1; NC_008533.2.
DR   SMR; A0A0H2ZPT5; -.
DR   STRING; 373153.SPD_1480; -.
DR   EnsemblBacteria; ABJ55292; ABJ55292; SPD_1480.
DR   GeneID; 60234370; -.
DR   KEGG; spd:SPD_1480; -.
DR   eggNOG; COG0849; Bacteria.
DR   HOGENOM; CLU_037850_1_1_9; -.
DR   OMA; DGIIRHT; -.
DR   OrthoDB; 1044637at2; -.
DR   BioCyc; SPNE373153:G1G6V-1596-MON; -.
DR   Proteomes; UP000001452; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02033; FtsA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR020823; Cell_div_FtsA.
DR   InterPro; IPR021873; FtsA_C.
DR   InterPro; IPR003494; SHS2_FtsA.
DR   Pfam; PF11983; DUF3484; 1.
DR   Pfam; PF02491; SHS2_FTSA; 1.
DR   PIRSF; PIRSF003101; FtsA; 1.
DR   SMART; SM00842; FtsA; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01174; ftsA; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell membrane; Membrane.
FT   CHAIN           1..457
FT                   /note="Cell division protein FtsA"
FT                   /id="PRO_0000454546"
SQ   SEQUENCE   457 AA;  49475 MW;  48F41D34E7D5FD92 CRC64;
     MAREGFFTGL DIGTSSVKVL VAEQRNGELN VIGVSNAKSK GVKDGIIVDI DAAATAIKSA
     ISQAEEKAGI SIKSVNVGLP GNLLQVEPTQ GMIPVTSDTK EITDQDVENV VKSALTKSMT
     PDREVITFIP EEFIVDGFQG IRDPRGMMGV RLEMRGLLYT GPRTILHNLR KTVERAGVQV
     ENVIISPLAM VQSVLNEGER EFGATVIDMG AGQTTVATIR NQELQFTHIL QEGGDYVTKD
     ISKVLKTSRK LAEGLKLNYG EAYPPLASKE TFQVEVIGEV EAVEVTEAYL SEIISARIKH
     ILEQIKQELD RRRLLDLPGG IVLIGGNAIL PGMVELAQEV FGVRVKLYVP NQVGIRNPAF
     AHVISLSEFA GQLTEVNLLA QGAIKGENDL SHQPISFGGM LQKTAQFVQS TPVQPAPAPE
     VEPVAPTEPM ADFQQASQNK PKLADRFRGL IGSMFDE