ID Q49VI8_STAS1 Unreviewed; 431 AA.
AC Q49VI8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Penicillin binding protein 4 {ECO:0000313|EMBL:BAE19222.1};
GN OrderedLocusNames=SSP2077 {ECO:0000313|EMBL:BAE19222.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE19222.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE19222.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; AP008934; BAE19222.1; -; Genomic_DNA.
DR RefSeq; WP_011303721.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49VI8; -.
DR KEGG; ssp:SSP2077; -.
DR PATRIC; fig|342451.11.peg.2070; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_5_0_9; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000006371; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
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:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.30.140.20; Penicillin-binding protein 4, C-terminal domain; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR015294; Pen-bd_prot4_C_dom.
DR InterPro; IPR037091; Pen-bd_prot4_C_dom_sf.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR NCBIfam; NF038258; PBP4_Staph; 1.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF09211; DUF1958; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000006371};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..431
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004235253"
FT TRANSMEM 399..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..285
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 314..378
FT /note="Penicillin-binding protein 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09211"
FT ACT_SITE 72
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 431 AA; 48455 MW; BA0382D9C02BA1AA CRC64;
MRKFILTIIT VLFVGTIITP FAQAESITPT QAANQYGYNV TDSYQPEGAI NVSQTGQLLY
QYNINKTWYP ASMTKLMTMY LTLEAVNKGD LSLNDKVKIT DEHYRMSTLP ELSNTKLYPG
ETYTIKELLQ ITVSNSSNAA ALILAKEVSG NLSDFTDKMN SKAKSLGMKD THFVNPTGAE
NKQLKDFAPK KYKNEDNNTS TAKDFGILSQ HAVQDTPKIL DFTKQLAPTQ HGVTYYTFNH
SLEGADMSLE GTDGLKTGSS DIADYNHTIT TKRDGFRINQ VIMGAGDYKN LGGEKQRNMI
GNGLMNMSFD QYKYTKILSK GEQKINGKTY FVEKDLYDVL PKDFDKNDYK VVIEDDKAHI
DYDREFISDK YGPPSVNVNK PLVHQATTIV KSSWDEHPIL TLLGTILIIV AIAIVIYLII
DLFRKKSRNK K
//
