ID A0A1F5C4N3_9BACT Unreviewed; 1160 AA.
AC A0A1F5C4N3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Calx-beta domain-containing protein {ECO:0000259|SMART:SM00237};
GN ORFNames=A2V45_03890 {ECO:0000313|EMBL:OGD37825.1};
OS Candidatus Aminicenantes bacterium RBG_19FT_COMBO_58_17.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797275 {ECO:0000313|EMBL:OGD37825.1, ECO:0000313|Proteomes:UP000178644};
RN [1] {ECO:0000313|EMBL:OGD37825.1, ECO:0000313|Proteomes:UP000178644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, 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:OGD37825.1}.
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DR EMBL; MEYD01000095; OGD37825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5C4N3; -.
DR STRING; 1797275.A2V45_03890; -.
DR Proteomes; UP000178644; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF07705; CARDB; 5.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00237; Calx_beta; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 459..557
FT /note="Calx-beta"
FT /evidence="ECO:0000259|SMART:SM00237"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1160 AA; 118276 MW; EF304567B7310FFF CRC64;
MKKRLHLSSF QIVLSVLILL AVFLAGAQNR PDRLYPALEQ RLQKLAPGEK LAVIVELDTQ
AKPLAVVSRM RGATRRAKAR AVVEALRSMA DQHQGPLREH LQKQRTAGAA ERIIPFWVFN
GFAVTATEPL IRSLASRPEV REIRLDVQIP VPSLSAARNA GPSPVTEWNL EQVRAPEVWA
LNPAYNGSGT VIGSFDTGVD LTHPDLHSRY RGNHQISWFD PYNEHAVPYD FHGHGTHTTG
IAVGGDSAGS SIGVAPGATW IAAKGWNDAG VGDASTFHQI FEWFLAPGGD PDNAPDVVNN
SWAFEEAGCL TEFLPDIEAW RAAGIFPAFA SGNDGPDPGS VRSPGAYPEA FAVGATDSSD
AVSDFSSQGP SPCDGSIKPD IAAPGEAVLS AVPWGYEILS GTSMATPHVA GAVAVLRSIA
AGLTVEQLES ALTSGASDIE DPGSDHASGA GRLDLFVSAQ VALHGPGFPV VKIAATDNTA
TEAGPTSGTI TITRAGDTDS DLEVKYSIGG TATSGSDYDP IPETMIIPAG SETSTVLITT
IDDLLAEVDE TVTLTIGPDS AYIVSAKDTA SVTIKSDELL SDLIITAFSA PATAAAGQTI
SLTDTTKNQG KGAADPSLTH FYLSTDNNPE SSDVLLGIRE VPALSAGASH PGSLTVTIPA
GTAAGTWYVI AKADGQGTVV ESSETNNKSA RSFIVGPDLD ITAFSAPAVA GAGQAIVVTD
TTKNAGAAAA GPSQTRFYLS ANSAFEASDA LIGSRSVPEL AAGASSSSST TVTIPQGTTV
GTWYVIANAD GEGVVAEAVE TNNTYARTIK IGPDLDITAL SAPAAAAAGQ TIVVTDTTKN
QGGGEAGPSV TQVFLSANGS VDPSDIRLGS RSVPALAAGT SSAGSMSITI PEGTAAGTWN
LIVKADGEGT VSETSESNNT SSRSLLVGPD LDITALSAPT AAAAGQTIVV TDTTKNAGAG
AAGPSLTQFY FSGNGAIDAS DIPIGSRSVT ALGAGESNSG STSLTIPEGT APKTWYIIAK
ADGEGVLAET SETNNTFTRT IYIGPDLAIT ALSAPATATA GQTISVGDTT KNKGAAGAEP
TLTEFYISAN SILDASDVLI GSRSVPTLAA GESSSGTTAV PVPLGTAAGT WYIIAKADAG
GAVAETWETN NTYSRSIKIN
//
