MACP_STRP2
ID MACP_STRP2 Reviewed; 104 AA.
AC A0A0H2ZNG3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Penicillin-binding protein 2a activator MacP {ECO:0000305};
DE Short=PBP2a activator MacP {ECO:0000305};
DE AltName: Full=Membrane-anchored cofactor of PBP2a {ECO:0000303|PubMed:29487215};
GN Name=macP; OrderedLocusNames=SPD_0876 {ECO:0000312|EMBL:ABJ54734.1};
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153 {ECO:0000312|EMBL:ABJ54734.1};
RN [1] {ECO:0000312|EMBL:ABJ54734.1, ECO:0000312|Proteomes:UP000001452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466 {ECO:0000312|Proteomes:UP000001452};
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, INTERACTION WITH PBP1A AND PBP2A, SUBCELLULAR LOCATION, DOMAIN,
RP PTM, DISRUPTION PHENOTYPE, TOPOLOGY, PHOSPHORYLATION AT THR-32, AND
RP MUTAGENESIS OF THR-32.
RC STRAIN=D39 / NCTC 7466 {ECO:0000303|PubMed:29487215};
RX PubMed=29487215; DOI=10.1073/pnas.1715218115;
RA Fenton A.K., Manuse S., Flores-Kim J., Garcia P.S., Mercy C.,
RA Grangeasse C., Bernhardt T.G., Rudner D.Z.;
RT "Phosphorylation-dependent activation of the cell wall synthase PBP2a in
RT Streptococcus pneumoniae by MacP.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:2812-2817(2018).
CC -!- FUNCTION: Required for the in vivo function of penicillin-binding
CC protein 2a (PBP2a), which is involved in the biosynthesis of cross-
CC linked peptidoglycan (PG) of the cell wall.
CC {ECO:0000269|PubMed:29487215}.
CC -!- SUBUNIT: Interacts with class A penicillin-binding proteins PBP1a and
CC PBP2a. {ECO:0000269|PubMed:29487215}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29487215};
CC Single-pass type IV membrane protein {ECO:0000305|PubMed:29487215}.
CC Note=Localizes to sites of new peptidoglycan (PG) synthesis at midcell
CC independently of PBP2a. {ECO:0000269|PubMed:29487215}.
CC -!- DOMAIN: C-terminal transmembrane domain is sufficient for its midcell
CC localization, but not for the full function.
CC {ECO:0000269|PubMed:29487215}.
CC -!- PTM: Phosphorylation by StkP is required for its ability to promote
CC PBP2a function. {ECO:0000269|PubMed:29487215}.
CC -!- DISRUPTION PHENOTYPE: Synthetically lethal with PBP1a. Deletion of this
CC gene with concomitant depletion of PBP1a leads to progressive reduction
CC in cell size before ultimate lysis. Cell wall synthesis is also
CC dramatically reduced in these cells. On the other hand, cells lacking
CC this gene are unaffected by the depletion of PBP2a.
CC {ECO:0000269|PubMed:29487215}.
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DR EMBL; CP000410; ABJ54734.1; -; Genomic_DNA.
DR RefSeq; WP_000520411.1; NC_008533.2.
DR AlphaFoldDB; A0A0H2ZNG3; -.
DR SMR; A0A0H2ZNG3; -.
DR STRING; 373153.SPD_0876; -.
DR EnsemblBacteria; ABJ54734; ABJ54734; SPD_0876.
DR GeneID; 60233880; -.
DR KEGG; spd:SPD_0876; -.
DR eggNOG; ENOG5030N27; Bacteria.
DR HOGENOM; CLU_152612_0_0_9; -.
DR OMA; QEFYDED; -.
DR OrthoDB; 2051627at2; -.
DR BioCyc; SPNE373153:G1G6V-962-MON; -.
DR Proteomes; UP000001452; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane;
KW Peptidoglycan synthesis; Phosphoprotein; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..104
FT /note="Penicillin-binding protein 2a activator MacP"
FT /id="PRO_0000452971"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29487215"
FT TRANSMEM 83..103
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29487215"
FT TOPO_DOM 104
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29487215"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29487215"
FT MUTAGEN 32
FT /note="T->A,E: Localizes to midcell and interacts with
FT PBP2a, but loss of activation of PBP2a."
FT /evidence="ECO:0000269|PubMed:29487215"
SQ SEQUENCE 104 AA; 11809 MW; 1D5F3AAAB85478B4 CRC64;
MGKSLLTDEM IERANRGEKI SGPPLLDDNE ETKILPTSSS RFGYANPKDH GFSQETLKIQ
VEPSIHKSRR IENTKRNVFN SKLNKILFAV IFLLILLVLA MKLL
