ID A0A0A1CU19_9MICC Unreviewed; 216 AA.
AC A0A0A1CU19;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=ART_1163 {ECO:0000313|EMBL:AIY00762.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY00762.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIY00762.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY00762.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
RL Submitted (APR-2014) 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|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP007595; AIY00762.1; -; Genomic_DNA.
DR RefSeq; WP_038463017.1; NZ_CP007595.1.
DR AlphaFoldDB; A0A0A1CU19; -.
DR STRING; 1494608.ART_1163; -.
DR KEGG; arm:ART_1163; -.
DR HOGENOM; CLU_028723_0_2_11; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000030301; Chromosome.
DR GO; GO:0016020; C: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; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:AIY00762.1};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000030301}.
FT DOMAIN 16..203
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 113
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 216 AA; 23355 MW; 0EC73AA884BE31C9 CRC64;
MTQAKRQSRK LGWRFVVLAV ALIFLFLALV RNVWMDVYYI PSESMEPLLL TGDRVLVSRL
AFTNEPIQRG DVVVFDGRGS FAPWKSGAGP VADGLVGAGQ WLGVLPNDNI YVKRVLGVAG
DTVKCCTPAG LLEINGVPVT ETYLYPGDAP SELPFEVIVP QGKLWLMGDH RSVSLDSRSL
LGAPGGGLIS SSMVIGSPVA NVWPLGRIHA IYSDKY
//