ID F2LV32_HIPMA Unreviewed; 164 AA.
AC F2LV32;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=Hipma_0646 {ECO:0000313|EMBL:AEA33616.1};
OS Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2).
OC Bacteria; Campylobacterota; Desulfurellia; Desulfurellales; Hippeaceae;
OC Hippea.
OX NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA33616.1, ECO:0000313|Proteomes:UP000008139};
RN [1] {ECO:0000313|EMBL:AEA33616.1, ECO:0000313|Proteomes:UP000008139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700847 / DSM 10411 / MH2
RC {ECO:0000313|Proteomes:UP000008139};
RX PubMed=21886857;
RA Huntemann M., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Rohde M., Spring S., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Mavromatis K.;
RT "Complete genome sequence of the thermophilic sulfur-reducer Hippea
RT maritima type strain (MH(2)).";
RL Stand. Genomic Sci. 4:303-311(2011).
RN [2] {ECO:0000313|Proteomes:UP000008139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700847 / DSM 10411 / MH2
RC {ECO:0000313|Proteomes:UP000008139};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Hippea maritima DSM 10411.";
RL Submitted (MAR-2011) 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; CP002606; AEA33616.1; -; Genomic_DNA.
DR RefSeq; WP_013681657.1; NC_015318.1.
DR AlphaFoldDB; F2LV32; -.
DR STRING; 760142.Hipma_0646; -.
DR KEGG; hmr:Hipma_0646; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_104604_1_0_7; -.
DR InParanoid; F2LV32; -.
DR OrthoDB; 5360818at2; -.
DR Proteomes; UP000008139; 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 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 SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000008139}.
FT DOMAIN 10..160
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 164 AA; 18784 MW; 86B3E8725A8BE5CF CRC64;
MWKSKKGIIT AAVLVVSLVF LHFILTHLSF SATDSVGYHL FYISKNFKKI KKHDYVLFPI
HETNIKEIQN ELKKFKTIIL VKQVACVPGD RLTVKGRKFY CNGQYLCTAK IRALDGEKIN
HFKFNGVVPN GYVFVLGKDV NSYDSRYFGF VPIKEVMAVA YPIL
//
