PBPX_STRR6
ID PBPX_STRR6 Reviewed; 750 AA.
AC P59676;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Penicillin-binding protein 2X;
DE Short=PBP-2X;
DE Short=PBP2X;
GN Name=pbpX; OrderedLocusNames=spr0304;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF MET-289; GLY-597 AND
RP GLY-601.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=2615650; DOI=10.1111/j.1365-2958.1989.tb00115.x;
RA Laible G., Hakenbeck R., Sicard M.A., Joris B., Ghuysen J.-M.;
RT "Nucleotide sequences of the pbpX genes encoding the penicillin-binding
RT proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant
RT mutant, C506.";
RL Mol. Microbiol. 3:1337-1348(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=8454182; DOI=10.1111/j.1574-6968.1993.tb05954.x;
RA Kell C.M., Sharma U.K., Dowson C.G., Town C., Balganesh T.S., Spratt B.G.;
RT "Deletion analysis of the essentiality of penicillin-binding proteins 1A,
RT 2B and 2X of Streptococcus pneumoniae.";
RL FEMS Microbiol. Lett. 106:171-175(1993).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=R6 / R704;
RX PubMed=23873916; DOI=10.1128/jb.00184-13;
RA Berg K.H., Stamsaas G.A., Straume D., Haavarstein L.S.;
RT "Effects of low PBP2b levels on cell morphology and peptidoglycan
RT composition in Streptococcus pneumoniae R6.";
RL J. Bacteriol. 195:4342-4354(2013).
CC -!- FUNCTION: A transpeptidase that forms peptide cross-links between
CC adjacent glycan strands in cell wall peptidoglycan (PG). Part of the
CC divisome machinery that synthesizes the septal cross wall. Beta-lactams
CC inactivate the PBPs by acylating an essential serine residue in the
CC active site of these proteins. {ECO:0000305|PubMed:23873916}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted (PubMed:8454182).
CC Cells depleted of PBP2x stop growing within a few hours after
CC expression stops. Cells are lemon-shaped rather than ellipsoid and some
CC are elongated (PubMed:23873916). {ECO:0000269|PubMed:23873916,
CC ECO:0000269|PubMed:8454182}.
CC -!- MISCELLANEOUS: The mature form of PBP2x contains an unprocessed signal
CC sequence followed by a membrane-anchoring segment.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR EMBL; X16367; CAA34412.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99108.1; -; Genomic_DNA.
DR RefSeq; NP_357898.1; NC_003098.1.
DR RefSeq; WP_000872267.1; NC_003098.1.
DR PDB; 1PYY; X-ray; 2.42 A; A=49-750.
DR PDB; 5OAU; X-ray; 2.67 A; A=49-750.
DR PDB; 5OIZ; X-ray; 2.70 A; A=49-750.
DR PDB; 5OJ0; X-ray; 2.66 A; A=49-750.
DR PDB; 5OJ1; X-ray; 2.85 A; A=49-750.
DR PDBsum; 1PYY; -.
DR PDBsum; 5OAU; -.
DR PDBsum; 5OIZ; -.
DR PDBsum; 5OJ0; -.
DR PDBsum; 5OJ1; -.
DR AlphaFoldDB; P59676; -.
DR SMR; P59676; -.
DR STRING; 171101.spr0304; -.
DR BindingDB; P59676; -.
DR ChEMBL; CHEMBL1255138; -.
DR DrugBank; DB03190; 6-o-Capryloylsucrose.
DR DrugBank; DB01147; Cloxacillin.
DR MEROPS; X52.001; -.
DR PRIDE; P59676; -.
DR EnsemblBacteria; AAK99108; AAK99108; spr0304.
DR GeneID; 60232761; -.
DR KEGG; spr:spr0304; -.
DR PATRIC; fig|171101.6.peg.341; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_1_9; -.
DR OMA; HGKEEYY; -.
DR EvolutionaryTrace; P59676; -.
DR PRO; PR:P59676; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS51178; PASTA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell cycle; Cell division;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..750
FT /note="Penicillin-binding protein 2X"
FT /id="PRO_0000195454"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 632..691
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 692..750
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT ACT_SITE 337
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD65"
FT MUTAGEN 289
FT /note="M->T: In C506; cefotamine resistant."
FT /evidence="ECO:0000269|PubMed:2615650"
FT MUTAGEN 597
FT /note="G->D: In C506; cefotamine resistant."
FT /evidence="ECO:0000269|PubMed:2615650"
FT MUTAGEN 601
FT /note="G->V: In C506; cefotamine resistant."
FT /evidence="ECO:0000269|PubMed:2615650"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5OJ1"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5OJ1"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5OIZ"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5OJ1"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5OJ1"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:5OIZ"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5OIZ"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 267..284
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:5OIZ"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 505..520
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:5OIZ"
FT STRAND 568..580
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 582..591
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 597..613
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:1PYY"
FT TURN 619..621
FT /evidence="ECO:0007829|PDB:5OJ1"
FT TURN 626..629
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 646..655
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 659..665
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 667..674
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 685..691
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 704..713
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 717..722
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 725..732
FT /evidence="ECO:0007829|PDB:1PYY"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:1PYY"
FT STRAND 742..749
FT /evidence="ECO:0007829|PDB:1PYY"
SQ SEQUENCE 750 AA; 82343 MW; 0699AF8081B25869 CRC64;
MKWTKRVIRY ATKNRKSPAE NRRRVGKSLS LLSVFVFAIF LVNFAVIIGT GTRFGTDLAK
EAKKVHQTTR TVPAKRGTIY DRNGVPIAED ATSYNVYAVI DENYKSATGK ILYVEKTQFN
KVAEVFHKYL DMEESYVREQ LSQPNLKQVS FGAKGNGITY ANMMSIKKEL EAAEVKGIDF
TTSPNRSYPN GQFASSFIGL AQLHENEDGS KSLLGTSGME SSLNSILAGT DGIITYEKDR
LGNIVPGTEQ VSQRTMDGKD VYTTISSPLQ SFMETQMDAF QEKVKGKYMT ATLVSAKTGE
ILATTQRPTF DADTKEGITE DFVWRDILYQ SNYEPGSTMK VMMLAAAIDN NTFPGGEVFN
SSELKIADAT IRDWDVNEGL TGGRMMTFSQ GFAHSSNVGM TLLEQKMGDA TWLDYLNRFK
FGVPTRFGLT DEYAGQLPAD NIVNIAQSSF GQGISVTQTQ MIRAFTAIAN DGVMLEPKFI
SAIYDPNDQT ARKSQKEIVG NPVSKDAASL TRTNMVLVGT DPVYGTMYNH STGKPTVTVP
GQNVALKSGT AQIADEKNGG YLVGLTDYIF SAVSMSPAEN PDFILYVTVQ QPEHYSGIQL
GEFANPILER ASAMKDSLNL QTTAKALEQV SQQSPYPMPS VKDISPGDLA EELRRNLVQP
IVVGTGTKIK NSSAEEGKNL APNQQVLILS DKAEEVPDMY GWTKETAETL AKWLNIELEF
QGSGSTVQKQ DVRANTAIKD IKKITLTLGD
