ID F9HGQ7_9STRE Unreviewed; 1946 AA.
AC F9HGQ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=M26 IgA1-specific Metallo-endopeptidase C-terminal domain protein {ECO:0000313|EMBL:EGP66139.1};
GN ORFNames=HMPREF9182_1706 {ECO:0000313|EMBL:EGP66139.1};
OS Streptococcus sp. oral taxon 056 str. F0418.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=904294 {ECO:0000313|EMBL:EGP66139.1, ECO:0000313|Proteomes:UP000004514};
RN [1] {ECO:0000313|Proteomes:UP000004514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0418 {ECO:0000313|Proteomes:UP000004514};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M26 family.
CC {ECO:0000256|ARBA:ARBA00005425}.
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:EGP66139.1}.
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DR EMBL; AFQU01000001; EGP66139.1; -; Genomic_DNA.
DR RefSeq; WP_009443582.1; NZ_AFQU01000001.1.
DR eggNOG; COG3064; Bacteria.
DR Proteomes; UP000004514; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR InterPro; IPR011098; G5_dom.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011505; Peptidase_M26_C_dom.
DR InterPro; IPR008006; Peptidase_M26_N_dom.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR Pfam; PF07501; G5; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF07580; Peptidase_M26_C; 1.
DR Pfam; PF05342; Peptidase_M26_N; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM01208; G5; 1.
DR PROSITE; PS51109; G5; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000004514};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 443..524
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT REGION 203..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1946 AA; 213486 MW; 5B7B1364EBD09243 CRC64;
MKRVGKAQEK IQKYSIRKLS VGIGSVVIAA MIFGSFLSSS IVAADEVGGS ETAHYTFIEE
QELTEQEKGL IKQGLPENLQ TGENYYLIYR KQDEKTVLPR TGNNGQPLLG LFAGTAILAV
LVFSRKKSGK LLGVLLLGSL GQAVLQSPQV FALENRELLS YNRQVTVSSA VSEEDVTIAG
YNYIGYFTAS DLLALTGTKP TSLPAGQEAR GQAELSEAAK EGSDANDQVA QSGLLDQLNS
ATSDSEQTGE HLAPNSSPAP APQSPNSAIE TAKGGSVQEP ALPEYSGATN GESLIQAEKP
VYTAPVDTSG DTAPVEPALP AYTGSVNGEP EVQPEKPAYT GPVGTAGDIA PVEPALPAYT
GSVNGEPEVQ PEKPAYTGPI GTSGDTAPVE PALPAYTGSV NGEPAVQPEK PAYTEPIGTA
GDTAPIELAL PEYTGGVNGE STVQAELPSL HTDVKLETIE PKIVHKTDDS KYLDEEATVE
GTPGQKEIVT SYEVLDGKRI SEPQTTERIL HEVVDTVVTR GSKARINKEE LSKQLALAAA
VDPGVYTNQS YQQLQAIKNM AESVYQTSSS QDEVDAGVNQ LKQALADLLA LKAAPTLTVS
GVKKDELQKS VQIQYQLTDR DQAFTSAHVR LKKDGQLIAE QNLAAGQLTT SFSGLDYYTP
YKIETTLSYD LGNGSESKEL AQETVQLDLK KVELKSITNV ALMKVENGQT KLMPTLAEKP
ANLDQYYLHF TSDQFKDTVL PVTSIEEVVV DNQPVFKIQA QLPDLLQRSA TGLQNSFDFY
LEKAKKREGN VYYDFQDLLD GIKENPSGTF ILARSISAKL IDKPANSKSY LPGEFKGQLI
GSQNGERHAI LDLAHPLFDT ITSGTVKDID FKRVNMVYPD SQAGDTIATI AARLKNKGVI
ENVNVQGYLE GRDHIAGLVN NIEGQSRVEN VSFKGQIKSK GGNSVTAGIA GTNAMSLVSR
AYVEADIWVK SGQNAGMLVA QNFTNYSGAG WGNWGKLTQS VAKGKLEDAG SRNAAGIAAS
IWPYGTINDT VSYATVVNGK ELFSSDNEIT DAWMGQKLQN LFGVKGQSSG TKTGKDAKFR
RLTEAEAEQK VKSYRITALE QTSANEVTTE KLNAAILRTS TYQDKPGYKA ENEQLYQNLE
RFMPFYNQEF LIHEANKLVD AGKAGDLLTK KVLSVQALKG NQFVAGGTDA DKILVHFADG
SKTIFNLQNQ ARFEQTALPE YQIAELGTVY TPNHSTAVKE NLLTQLTESL KSFELYSDEV
YRSVGLPNDN DRVNKVKRLF LDESLAEVKA NLQDMISKLL ANEWTRFHAD NPAANEALKA
KIEENKTAIM LGLTYLNRYY DLKFGDYNLK ELVLFKPDFY GEKVPLLDRL IKIGRSTENQ
LKGADNVNMF ARQLKAESKS NDLVAYLDYN RRLLTDFADM DSWFKDATRG FIQFEERQSE
VEEIKSAKYR VFDNLNSEYF SNYILPLLTL KNTRLAILSN YSTMAFVNRD KRRSWSDERF
DARIKEVATQ HRNHVDTWYK LLSDDIKSRM VKQNVTAVWD GFDVEGRGWI DVNGNDNKGK
PYAPSREFFN LVGGRAGGWY KSNGYGAHAA GSIRVNFEAF DLLTEYGVSV FTHELTHVND
SYIYLGGHGR RQGIGPEGYA QGLLQSPVPG QPGWGALGLN MAFERPNDGS LIFNSSPSLF
KNRADIDHYM KGYNDTLMLL DYLEGQAVVD KGNAAAAKWF KKVEPKVVDA RTQYDVVREL
TAEEKAAMSV SSVNDLVDQG LLSNRAVDNR TYNPADYDSS YIAIDFMTGI YGGGQNNTGA
PGALMFKHNT FRIWGYYGYE KGFISYASNK HRKTANEQGV TGLSDNFIIN QISGGEFQTM
EAFKKAYFRK VVDKAQTSGI KSVTINGKVY STYEELKAGF AEAVDKDLKK SRVDERATKD
FKYAVFTQLL KNTNSFMDEN SIWGSK
//
