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Database: UniProt
Entry: E1SNP9_FERBD
LinkDB: E1SNP9_FERBD
Original site: E1SNP9_FERBD 
ID   E1SNP9_FERBD            Unreviewed;      1294 AA.
AC   E1SNP9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADN76722.1};
GN   OrderedLocusNames=Fbal_2520 {ECO:0000313|EMBL:ADN76722.1};
OS   Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN76722.1, ECO:0000313|Proteomes:UP000006683};
RN   [1] {ECO:0000313|EMBL:ADN76722.1, ECO:0000313|Proteomes:UP000006683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC   {ECO:0000313|Proteomes:UP000006683};
RX   DOI=10.4056/sigs.1161239;
RA   Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA   Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA   Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT   "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL   Stand. Genomic Sci. 3:174-182(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; CP002209; ADN76722.1; -; Genomic_DNA.
DR   STRING; 550540.Fbal_2520; -.
DR   KEGG; fbl:Fbal_2520; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_262126_0_0_6; -.
DR   OrthoDB; 614750at2; -.
DR   Proteomes; UP000006683; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04818; PA_subtilisin_1; 1.
DR   Gene3D; 2.60.40.3440; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   InterPro; IPR017312; Subtilisin_Alteromonadales.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PIRSF; PIRSF037898; Subtilisin_rel_Sputw3181_3341; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000006683};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1265..1283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          180..622
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          420..507
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          669..747
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        255
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        586
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1294 AA;  137701 MW;  ABCDA1650772F093 CRC64;
     MRLSVKSVGL IVCLLGGVGW LERAGASEAF ALQSMREHWS VSQRSSASEP SQRYIVQLDS
     EPVAWFLHQD DDPAAHGGKG SPLFSAASQR YRQKLMREAD QFERGLTNSR LDLKVKHRFT
     SLFNGVVLEG HQIDVAQVAA MQGVRAVFPE RLFYTNLDTS LELIDAPGAW RRVGGRDDAG
     AGVRVAIIDS GIRPEHPMFS SVGFTAPEKG MPSDDYCSEQ DASFCNGKLI VARWYMPSMN
     IWQDEHRSPL GFNGHGTHVA AIAVGNRVEV DHKGNRFTLS GVAPGAYLMV YKALFSPAYD
     PTRAMGSNIT LLQALEDAVN DGADVINNSW GGGIGLDPAF SPFHKALIAA EAAGVVVVSS
     AGNAGPEPGT ISCPGCVASG LAVANTTHGR YISNVLSLGN LPDVYALEGT SSIRVSEDIS
     APLVAADQVD PGNSKGCRPF AQESFRDSIA LVQRGDCPFL DKSEHALLAG AKALVVDNHQ
     SGEPFGMLMD KARIPAVMVD QASGAMLRAA LLKGSTALAT ISATEHPVVS ESLVDMVHTS
     SSRGPNGDPN ILKPDIAAPG ALILSAVSSQ EPGYEGQAVA MLTGTSMASP HVAGAAAVLK
     NLHPNWGAQA IKSALTSSAQ TEGLRLPDST SSPTPFDVGA GRLDLAAAAA AKLTFSATGF
     SDATCILQCQ FSTRVTNRSS NKGTWVVSTA LEGAEVTTQP TQLVLASGES AELVVTVDST
     LAKKGQWLFG RVELTAADNH AHLPIAVYPD ISDDLNLTAI YSAEPEHQLG EQAQYHAVLF
     NRAFNGPVTV TLDIDDALSI EPDSIETQLL GGLEQEVTVD TQRRRLVWQG RLNQTIASIT
     EVPPLAQNSL ASEANRIPCF GSCDEVSLVY TTALPFEFHG RSYNQFTVSS NGFLSPGETK
     ANSSWLNHRL PDSLVPNNVI APFWTDLDLQ DEDALPGNGS GGGTLHLYQV KDGAGEVNYL
     VVDWIGTQLA GHGDGEGYSF GVWLGVGQKK GHNLLRYYKL GPLPANLTVG VEDVLGAAGV
     MRYHNGEGVA PKEGDTLKVE MIPAGQLAID FSLSSVLPEA ISVTTKEDNP VSVKLLPSGS
     HPLVMTAENQ ENRVEAVRLV DFGIDEGVSV RVLNAPDAGI VQPQGSSIVY QPEADFSGQD
     RVRYELLDGG GNALFQQQLV IDVTQVNDAP RINMPLSYQV RSGEQLEVGL RASDVEGDPI
     QWQVTQRQGT AVDTEIVGST MIVMAPTVQQ AETVVLALVA SDPQVSSQPV MLNIKIWPVE
     GEEESGGGVM SGVVLAILLW LLASRGWCYR RRAH
//
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