ID A0A0X8FKQ6_9LACT Unreviewed; 192 AA.
AC A0A0X8FKQ6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=AWM75_03350 {ECO:0000313|EMBL:AMB99095.1}, SAMN04487985_10428
GN {ECO:0000313|EMBL:SDM03466.1};
OS Aerococcus urinaehominis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=128944 {ECO:0000313|EMBL:AMB99095.1, ECO:0000313|Proteomes:UP000062260};
RN [1] {ECO:0000313|EMBL:AMB99095.1, ECO:0000313|Proteomes:UP000062260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG42038B {ECO:0000313|EMBL:AMB99095.1,
RC ECO:0000313|Proteomes:UP000062260};
RX PubMed=27103727;
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT and Aerococcus viridans CCUG 4311T.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000062260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG42038B {ECO:0000313|Proteomes:UP000062260};
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT Illumina Hiseq.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SDM03466.1, ECO:0000313|Proteomes:UP000183325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15634 {ECO:0000313|EMBL:SDM03466.1,
RC ECO:0000313|Proteomes:UP000183325};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606,
CC ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|RuleBase:RU362042}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014163; AMB99095.1; -; Genomic_DNA.
DR EMBL; FNHJ01000004; SDM03466.1; -; Genomic_DNA.
DR RefSeq; WP_067978204.1; NZ_FNHJ01000004.1.
DR AlphaFoldDB; A0A0X8FKQ6; -.
DR STRING; 128944.AWM75_03350; -.
DR KEGG; auh:AWM75_03350; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000062260; Chromosome.
DR Proteomes; UP000183325; Unassembled WGS sequence.
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 Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR PANTHER; PTHR43390:SF8; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000062260};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 13..163
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 192 AA; 21523 MW; F5F26741EE6AA757 CRC64;
MKNNWMKELL INVLIVVVTF AAVFLLFKYV AGPVRVSGQS MESSFQDGDR LLDAQLTDIS
HFDVVVFDAP DGSGDKYIKR VIGLPGDHIA FKNDVLYLNG QPYEEPYIDK SLNPTDGPNT
FDFDLAQLTG SSQVPEGKAF VMGDNRQNSN DSRYFGFIDL DQLSEIKYEF WPTDDFGSVP
NYEIQSGQIV AE
//
