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Penicillin-binding protein PbpB (Penicillin-binding protein 3) (PBP3)

 PBPB_MYCTU              Reviewed;         679 AA.
L0T911;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
23-MAY-2018, entry version 31.
RecName: Full=Penicillin-binding protein PbpB;
AltName: Full=Penicillin-binding protein 3;
Short=PBP3;
Name=pbpB; Synonyms=ftsI, pbp3; OrderedLocusNames=Rv2163c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TOPOLOGY, INTERACTION
WITH WAG31, CLEAVAGE BY RIP1, AND MUTAGENESIS OF ALA-102; ALA-103;
427-HIS--VAL-429 AND 488-GLN--SER-490.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19496931; DOI=10.1111/j.1365-2958.2009.06750.x;
Mukherjee P., Sureka K., Datta P., Hossain T., Barik S., Das K.P.,
Kundu M., Basu J.;
"Novel role of Wag31 in protection of mycobacteria under oxidative
stress.";
Mol. Microbiol. 73:103-119(2009).
-!- FUNCTION: Synthesis of cross-linked peptidoglycan from the lipid
intermediates. {ECO:0000250, ECO:0000269|PubMed:19496931}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBUNIT: Interacts with Wag31. {ECO:0000269|PubMed:19496931}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}.
-!- DOMAIN: The enzyme has an N-terminal penicillin insensitive
transglycosylase domain (formation of linear glycan strands) and a
C-terminal penicillin-sensitive transpeptidase domain (cross-
linking of the peptide subunits). {ECO:0000250}.
-!- PTM: Cleaved by Rip1 in response to oxidative stress (H(2)O(2)),
prevented by Wag31. Cleavage probably occurs near residues 102-
103.
-!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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EMBL; AL123456; CCP44940.1; -; Genomic_DNA.
RefSeq; NP_216679.1; NC_000962.3.
RefSeq; WP_003411214.1; NZ_KK339370.1.
ProteinModelPortal; L0T911; -.
SMR; L0T911; -.
STRING; 83332.Rv2163c; -.
PaxDb; L0T911; -.
EnsemblBacteria; CCP44940; CCP44940; Rv2163c.
GeneID; 887949; -.
KEGG; mtu:Rv2163c; -.
TubercuList; Rv2163c; -.
eggNOG; ENOG4105CJN; Bacteria.
eggNOG; COG0768; LUCA.
InParanoid; L0T911; -.
KO; K03587; -.
OMA; NVGMIKI; -.
PhylomeDB; L0T911; -.
UniPathway; UPA00219; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR005311; PBP_dimer.
InterPro; IPR036138; PBP_dimer_sf.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF03717; PBP_dimer; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF56519; SSF56519; 1.
SUPFAM; SSF56601; SSF56601; 1.
1: Evidence at protein level;
Cell membrane; Cell shape; Cell wall biogenesis/degradation;
Complete proteome; Membrane; Peptidoglycan synthesis;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 679 Penicillin-binding protein PbpB.
/FTId=PRO_0000422679.
TOPO_DOM 1 90 Cytoplasmic.
{ECO:0000305|PubMed:19496931}.
TRANSMEM 91 111 Helical. {ECO:0000255}.
TOPO_DOM 112 679 Extracellular.
{ECO:0000305|PubMed:19496931}.
ACT_SITE 386 386 Acyl-ester intermediate.
{ECO:0000250|UniProtKB:P0AD65}.
MUTAGEN 102 103 AA->LL: No degradation by Rip1.
MUTAGEN 102 102 A->L: No effect on degradation by Rip1.
{ECO:0000269|PubMed:19496931}.
MUTAGEN 103 103 A->L: No effect on degradation by Rip1.
{ECO:0000269|PubMed:19496931}.
MUTAGEN 427 429 Missing: Decreased interaction with
Wag31. Loss of interaction, reduced
protection from Rip1 proteolysis; when
associated with 488-Q--S-490 deletion.
{ECO:0000269|PubMed:19496931}.
MUTAGEN 488 490 Missing: Decreased interaction with
Wag31. Loss of interaction, reduced
protection from Rip1 proteolysis; when
associated with 427-H--V-429 deletion.
{ECO:0000269|PubMed:19496931}.
SEQUENCE 679 AA; 72537 MW; 3FE57B17A4D265C4 CRC64;
MSRAAPRRAS QSQSTRPARG LRRPPGAQEV GQRKRPGKTQ KARQAQEATK SRPATRSDVA
PAGRSTRARR TRQVVDVGTR GASFVFRHRT GNAVILVLML VAATQLFFLQ VSHAAGLRAQ
AAGQLKVTDV QPAARGSIVD RNNDRLAFTI EARALTFQPK RIRRQLEEAR KKTSAAPDPQ
QRLRDIAQEV AGKLNNKPDA AAVLKKLQSD ETFVYLARAV DPAVASAICA KYPEVGAERQ
DLRQYPGGSL AANVVGGIDW DGHGLLGLED SLDAVLAGTD GSVTYDRGSD GVVIPGSYRN
RHKAVHGSTV VLTLDNDIQF YVQQQVQQAK NLSGAHNVSA VVLDAKTGEV LAMANDNTFD
PSQDIGRQGD KQLGNPAVSS PFEPGSVNKI VAASAVIEHG LSSPDEVLQV PGSIQMGGVT
VHDAWEHGVM PYTTTGVFGK SSNVGTLMLS QRVGPERYYD MLRKFGLGQR TGVGLPGESA
GLVPPIDQWS GSTFANLPIG QGLSMTLLQM TGMYQAIAND GVRVPPRIIK ATVAPDGSRT
EEPRPDDIRV VSAQTAQTVR QMLRAVVQRD PMGYQQGTGP TAGVPGYQMA GKTGTAQQIN
PGCGCYFDDV YWITFAGIAT ADNPRYVIGI MLDNPARNSD GAPGHSAAPL FHNIAGWLMQ
RENVPLSPDP GPPLVLQAT


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