LEP_STAAC
ID LEP_STAAC Reviewed; 191 AA.
AC Q5HHB9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Signal peptidase IB;
DE Short=SPase IB;
DE EC=3.4.21.89;
DE AltName: Full=Leader peptidase IB;
GN Name=spsB; OrderedLocusNames=SACOL0969;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Essential for cell viability. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW37937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000046; AAW37937.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000711486.1; NC_002951.2.
DR PDB; 4WVG; X-ray; 2.05 A; A=26-191.
DR PDB; 4WVH; X-ray; 2.10 A; A=26-175.
DR PDB; 4WVI; X-ray; 1.90 A; A=26-175.
DR PDB; 4WVJ; X-ray; 1.95 A; A=26-175.
DR PDBsum; 4WVG; -.
DR PDBsum; 4WVH; -.
DR PDBsum; 4WVI; -.
DR PDBsum; 4WVJ; -.
DR AlphaFoldDB; Q5HHB9; -.
DR SMR; Q5HHB9; -.
DR MEROPS; S26.016; -.
DR EnsemblBacteria; AAW37937; AAW37937; SACOL0969.
DR KEGG; sac:SACOL0969; -.
DR HOGENOM; CLU_028723_5_0_9; -.
DR Proteomes; UP000000530; 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR PANTHER; PTHR43390; PTHR43390; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Membrane; Protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..191
FT /note="Signal peptidase IB"
FT /id="PRO_0000109526"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 36
FT /evidence="ECO:0000250"
FT ACT_SITE 77
FT /evidence="ECO:0000250"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:4WVI"
FT TURN 36..40
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4WVI"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4WVI"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4WVG"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4WVI"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4WVI"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:4WVI"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4WVI"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4WVI"
SQ SEQUENCE 191 AA; 21678 MW; 1C7AEB108F88D7B5 CRC64;
MKKEILEWII SIAVAFVILF IVGKFIVTPY TIKGESMDPT LKDGERVAVN IVGYKTGGLE
KGNVVVFHAN KNDDYVKRVI GVPGDKVEYK NDTLYVNGKK QDEPYLNYNL KHKQGDYITG
TFQVKDLPNA NPKSNVIPKG KYLVLGDNRE VSKDSRAFGL IDEDQIVGKV SFRFWPFSEF
KHNFNPENTK N
