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Database: UniProt
Entry: U7D7T5_9BACT
LinkDB: U7D7T5_9BACT
Original site: U7D7T5_9BACT 
ID   U7D7T5_9BACT            Unreviewed;       889 AA.
AC   U7D7T5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:ERP39015.1};
GN   ORFNames=CALK_0507 {ECO:0000313|EMBL:ERP39015.1};
OS   Chitinivibrio alkaliphilus ACht1.
OC   Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC   Chitinivibrionaceae; Chitinivibrio.
OX   NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP39015.1, ECO:0000313|Proteomes:UP000017148};
RN   [1] {ECO:0000313|EMBL:ERP39015.1, ECO:0000313|Proteomes:UP000017148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACht1 {ECO:0000313|EMBL:ERP39015.1,
RC   ECO:0000313|Proteomes:UP000017148};
RX   PubMed=24112708;
RA   Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA   Muyzer G., Mardanov A.V., Ravin N.V.;
RT   "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT   extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT   candidate phylum Termite Group 3.";
RL   Environ. Microbiol. 0:0-0(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERP39015.1}.
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DR   EMBL; ASJR01000003; ERP39015.1; -; Genomic_DNA.
DR   RefSeq; WP_022636043.1; NZ_ASJR01000003.1.
DR   AlphaFoldDB; U7D7T5; -.
DR   STRING; 1313304.CALK_0507; -.
DR   PATRIC; fig|1313304.3.peg.487; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG3266; Bacteria.
DR   eggNOG; COG3511; Bacteria.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000017148; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04843; Peptidases_S8_11; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR044060; Bacterial_rp_domain.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034073; Subtilisin_DY-like_dom.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF18998; Flg_new_2; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ERP39015.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017148};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..889
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004679005"
FT   DOMAIN          633..784
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
SQ   SEQUENCE   889 AA;  98233 MW;  F97C4E1D869665CC CRC64;
     MFKFLLTLAW VSSIAYSGTL SGQNSLTPGV DAYRLLVKFS PDYVWDVDED KIYFSRLRTI
     SPEKNTFIDS FSYDQAVRYT PQEQEIMRRG ETPPPAQNRV DLSFFRGMVY VREAEELTPE
     EVLDLAEEFE QLSFVEYTAL EPVDPPPPPA IESPQNIPDF TWRQFYRKYN HGNDTIGINI
     DYAWNRGIYG QGVRVADIEW GFDYDHVDLA ADNFVELIST TDNSNDDHGT AVAGVMVAHD
     NGFGVTGMVH EVDTFYGISE IRHGRVTGIT EGLRRLRAGD VFLYEMQTGG QGGEFVPADY
     NQAVWDITQE ASDAGVIIVA AAGNGGENLD DPFYNSYNAR GDNGAIIVGA GTIQGRNRAG
     FSTYGSRVNL QGWGDWSVMT TGYGALHNGG PHATYTGSFS GTSSATPIVA SAVVAVQSFA
     KNELDLLLTP QEMRELLIET GTAQGSGWGA ENIVPQPNVQ AAIEWLENEH GTLPRYTLHA
     TAENGTVDMD PQKSRYDSGS VVTLTAEADE GYTFTEWTGD LSGDESPTTL VVNDNKHVEA
     HFSYTGEELS LETTMQDRMF ATETSHTIQW SSTNIDDSIH LILIHPTGTL DTIETDLSPN
     QEYEWDIDKK LPTATGYRLS ITSANSADTS QKFSLIQTTL AEDMVLIDQE TISIESVSSE
     ETHGEQAYAT NLLDMSTATR WHTAWLDSST GEWFDPAPSH PHTIVFDLDT LYGATGFAHT
     PRLDESTNSL IHEYLLEGST DGTAWDTISV GAFDWSEKRD IVTVGFPRTP ARYIRFTTRS
     TYEGSNNPGY ASGLQMNFFA DPSWEDPTPV VHENRPKEGI LFSQGTVHLT LDEPVKIHIT
     SVTGRRIAEI ASPGTATLNL REKNIPAGVY LFRIMTDAGI IQTQQIRLP
//
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