ID H6L8N2_SAPGL Unreviewed; 1236 AA.
AC H6L8N2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Metalloprotease, putative {ECO:0000313|EMBL:AFC26757.1};
GN OrderedLocusNames=SGRA_4042 {ECO:0000313|EMBL:AFC26757.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC26757.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC26757.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC26757.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family.
CC {ECO:0000256|ARBA:ARBA00006006}.
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DR EMBL; CP002831; AFC26757.1; -; Genomic_DNA.
DR RefSeq; WP_015694339.1; NC_016940.1.
DR AlphaFoldDB; H6L8N2; -.
DR STRING; 984262.SGRA_4042; -.
DR KEGG; sgn:SGRA_4042; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_007507_0_0_10; -.
DR OrthoDB; 5377264at2; -.
DR Proteomes; UP000007519; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09596; M36; 1.
DR CDD; cd04818; PA_subtilisin_1; 1.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR044023; Ig_7.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR NCBIfam; NF038113; T9SSA_dep_M36; 1.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF19081; Ig_7; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR Pfam; PF18911; PKD_4; 2.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR PROSITE; PS50093; PKD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AFC26757.1};
KW Metalloprotease {ECO:0000313|EMBL:AFC26757.1};
KW Protease {ECO:0000313|EMBL:AFC26757.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007519};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1236
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003604090"
FT DOMAIN 780..863
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1092..1145
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 1236 AA; 132117 MW; ECFF57032901EE03 CRC64;
MQNNLLLPTL LLLLFCGGQV RAQTSQEQIQ QLLLGEQKQL GLSPSDLSEW RVYDRHQSKQ
TGVEHIYIRQ MYQGIEVQNA VINLNIKDGQ LISLGNRFEA NLAQRVLAGS AQITPAAAIQ
KAADALYLPP LQDLRELENS GANSYLFSPA GISLENIPLK LCYQPGPEGE IRLAWDLSIH
QTNKQHWWSL RIDAQNGEIL AQEDWVKHCS FADHAFGNCS RPDVPHLPTV SGTLANNALP
AQYRVFAEPL ESPNHGSRTL EVDPADTTAS PLGWHDTDGQ AGAEYTITRG NNVHAYEDRA
AADQPGYSPD GGSALNFDFP LNMNQQPAAY EDAAITNLFY WNNLTHDVWY HYGFDEASGN
FQENNYGRGG QGGDYVFAEA QDGGGTNNAN FGTPPEGSNP TMQMFLWTNG GGATSLLDVN
SPSSIAGTYT ATEGTFGPNV PTTPITEDLV LADDATAPDP NDACDPLTNA ASLNGKIAVV
YRGSCTFVAK VQAAEAAGAL AVIVINNTAG APITMGGTGT TNIPSIMISD TDGAAIVAEM
ANGTVNASIG NFSANFDKDG DFDNGIIAHE YGHGISTRLT GGASNSGCLS NAEQMGEGWS
DYFGLMMTIE PGDQATDVRG IGTFANGQAV SGTGIRPAPY TTDMAINSYT YGDVNNTNLS
EPHGVGFVWA TVLWDLNWAL IDQYGYDADL YNGTAGNNMA MNLVINGIKL QPCGPGFVDG
RDAILQADQL LYGGANQCLI WEVFARRGLG ASADQGSSNN RSDQTEAFDL PTSCQTPVTA
PTANFNSLLV SACGSSVNFE DQSTDVPQQW RWDFGDGNTD TLPNPSHNYS ANGTYNVVLI
VSNSLGSDTI SSTVTISIPS APTAANQTIC PGSTTISANT SSNSVIWYDA QGTPLDTSLT
FVTPNLNSNT TYQMEGVTFY PKSFVGIDSA GASGNGGYHN TGFTGTQNFE AFKPLVIVSG
WIDAGSAGPR TIYLWDGNGN IVDQVTINAV RGPQRVELGL EVPSPGNYSL GGTYTDLFRN
NAGASYPYVV PGLLSINSSS ATTGPLDFWY YVYDWEVEEA PCRSPLGNLS VNVNNGAVFS
YTASDLDLSF TDQSANASSW AWDFGDGNSS TLQNPTHSYN LPGTYTITLS VNGNSSCVYS
ETITVAASSI QNLANGNSMQ LQPNPAKEIS TLSFSQPLES EQRLELISLD GRLLNSWQLA
IGQSRLEIDL EQLVPAFYIL RLTDKNGSHS LRLLVQ
//
