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Database: UniProt
Entry: A0A369AFR0_9FIRM
LinkDB: A0A369AFR0_9FIRM
Original site: A0A369AFR0_9FIRM 
ID   A0A369AFR0_9FIRM        Unreviewed;      3372 AA.
AC   A0A369AFR0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=RHS repeat-associated protein {ECO:0000313|EMBL:RCX08180.1};
GN   ORFNames=DFR58_1448 {ECO:0000313|EMBL:RCX08180.1};
OS   Anaerobacterium chartisolvens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerobacterium.
OX   NCBI_TaxID=1297424 {ECO:0000313|EMBL:RCX08180.1, ECO:0000313|Proteomes:UP000253034};
RN   [1] {ECO:0000313|EMBL:RCX08180.1, ECO:0000313|Proteomes:UP000253034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27016 {ECO:0000313|EMBL:RCX08180.1,
RC   ECO:0000313|Proteomes:UP000253034};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       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:RCX08180.1}.
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DR   EMBL; QPJT01000044; RCX08180.1; -; Genomic_DNA.
DR   OrthoDB; 9771173at2; -.
DR   Proteomes; UP000253034; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 3.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   Gene3D; 2.180.10.10; RHS repeat-associated core; 7.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR045351; DUF6531.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034204; PfSUB1-like_cat_dom.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR031325; RHS_repeat.
DR   InterPro; IPR006530; YD.
DR   NCBIfam; TIGR03696; Rhs_assc_core; 1.
DR   NCBIfam; TIGR01643; YD_repeat_2x; 4.
DR   PANTHER; PTHR45632; LD33804P; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF20148; DUF6531; 1.
DR   Pfam; PF01344; Kelch_1; 12.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF05593; RHS_repeat; 7.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00612; Kelch; 12.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF117281; Kelch motif; 3.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 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}; Reference proteome {ECO:0000313|Proteomes:UP000253034};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..3372
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016811228"
FT   DOMAIN          3187..3326
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          3206..3355
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   REGION          3064..3088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3109..3136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3152..3194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        255
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        411
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   3372 AA;  373300 MW;  0DF9449B2911AF4D CRC64;
     MKIKSFLNKA ILITLIACLF FVPRYIQAAD GTMLKAGVGK NGGISYSERK TDRFIIKYKN
     EKNRATEARN TKNGIMAANM PELKNYDVVT TKTRMKSSEL LAEIENKSTY GIEYIQPDFE
     MTISSEDPQY TNQWGMYSKY SAIPDVNTLP DDEKIRQFIL EDAKSMGLPS IRIDANVPAA
     WEKADGSGVM VAVLDTGIDI THEDISGNIS VNVAEIPGNG IDDDGNGYID DVSGWNFCDN
     NNTVHSKETE CDEWHGSHVA GIIAASKDNG KGIAGVAPAA KVLPLKVFKG GRAYTSDIIA
     AIQYAGKMGA KVVNCSWGST EYNQALKDAI EHSDMLFVCA AGNSHTDIDN NPVYPAAFDC
     KNIITAASID KNGVLSGFSN YGKASVDIAA PGNEIISTLP GNAYGKSSGS SMAAAFVSGE
     AALLSDMLKG ISIADLKNRI INSSDRLSSL TDKLGGGGKL NCGNAVSGIN KDEIVQIAFS
     DNDPCDSSSQ PEQGYELLAT DSWAGKASMP TARHNFGSAE TGGFIYAIGG NKSTYLNTVE
     EYDPVLNNWK TKAAMPTVRE CLSVVAAYGK IYAIGGYNGN YLNTVEEYDP ASDKWIAKAG
     MNTARQSAGA CVVNGKIYVI GGYNGNYLNT VEEYNPLTNS WRTLASMSAP RSQLGVAAVN
     GKVYAVGGYY LNQYLNTVQE YDPSTNVWAG KRAMPTARGS FGVSVVNSKI YAVGGICGSG
     CLNNAEEYNP ALDTWIAKTP MQIGKCNIST TSVNGRIYIM GGYNAGSLSS TEEYTPASDV
     WVTKAPMPTA RGFAGVAAID GRIYVAGGTY EGSSALEYKA INTFEEYDTE KNTWSVKPSM
     PTPRFGVGGA SAYGEFYAIG GWNWDINGNL DINSISKDTV EAYNPATGRW VSKASMGSQR
     FAPGVVELDG KIYAIGGAGQ KSAEVYNPLT NRWTPIADMS EARYGLAVAA VNGKIYVMGG
     YDYIFDKNLS DTVEEYNPST NTWTKKASMP TKRNYMGAVA VNGKIYIIGG NSGKYINNVD
     IYDPATDRWT TGTGMSVGRM RLGTVMVNGR IYAIGGYNGS YLSTVEEYSA EYDRYIMQTH
     FGEDGTNPAS GNFSRSYTDM SMDVPGFKLN IGRTYNSRND KSGPLGKGWT FSFEGNIKDD
     PNDSTLKVVT LPDGSVQTFK KSKDAGSNDI FTAKDSRSRL ELKAGGSYVL TTKDQYSYTF
     INGWLTLMQD KFGNTVSISV DSNGKISKIT DIAERSITVD YSGTSFIRFV KDVSGGRTVE
     YQYENNQLVR AIDPAGNITR YSYDSSGYMN GVKDHNSNRI EDLVYNHSAG DNQHKVSRIT
     DAYGNIFKYA YDNANKEASI TDSNGRQTVQ HYDSYMYTSS SRDAEGKEEI TEYNLDINGG
     NRFGEERAVT DRNGNKTAYD RDGRGNITKI TNPDGSTIEY TYDAKNNVIS EKNEQNKYTF
     YIYDAGMVYL LKKIEPLNGT DLYYQGCDES KFAITGYTYY TSQECQSNGY KAKGLLKENK
     SPEGKITAYT YYSNGCLKTE KDAQGKTTVH NYNSIGWETS TISPMKFKTE YFYDNNGRLE
     KTVANDGDGS AKPITTSSVT RTTYNIMGRK TQEVSPNLYD PAKDSLTSHT YTGNHGYRYV
     YNADYTLKRV TDPENNVTEY LTYDMYGNVL KEKKPNGAVY EYAYDALNRI KKVYFRENAS
     ASSTLLEEYS YDIVNGTTLQ NGAILKNTRK TRTVYLNDKE AAVTKYIYDY AGRLINQQNA
     DGTSSSIEYY LDGRVKSTTD ESLNKTYYKY GTYDSANNFR YDEKWALIEK SGSDALYTYS
     AVVYDKTGRI KSEKTGKQKV SLWNAPSDFV TKTYEYYGND KVYSITFNDG RKTQYQYDDD
     GNVSREEVYT DSTNKRTTLY ENNQFGLPCK KKVYVKLGDI YDCDFSSTFE ILPTTELAYD
     KNGNLKSVKT PEFVTTIYEY DNMDRRTSTS QSGYDEYMNA AVISASTLYN WEGKPIEATD
     TKGNKTFYHY NARGFLEKVE ETAAVNGADA RLYTLYGYDN AGRKIYEVSP KNYFPGQSVQ
     SMDRTEYTYD LMGRIKTQNE VFREKTVDPG DNSKWITSWV TITSKAYKYD SMGNIVKELD
     SLGYEAGTGT TADQKINTGY GTVYTYNCQG KVQTVLDPVS KDRGLAYSTK YEYDGMGRKV
     YEISAKGSGS GTYYSSTGYE YDDAGNVTEV RTKKNINDTG SSGQLVQVYT YDLMGNLLTR
     KDGNSNVTTF EYNAMGKLRK VIYPGDASIP SDIVIYQYDL VGNLKKQQNS LDTVDLYTYD
     NQGRVLSHTQ KKKDSSQTIT TSIRYDKNGN KRFETDGNGV KRENTYDQAD RLISTKITVT
     GERNRKTQKV TSYEYDANGN ATVTTDWRGN RYTSEYDPIN RLIEKSGPYG VIQKLEYNHN
     SSQKISYDAL YNITAFEYDK DNRLINTIDP EGHISLQSYD NAGNIGTRTD GRGNKTTYAY
     DEFNRLEKVT DATGQETSYS YDLNGNMLTQ TDAKGNTIAF EYNVRNKAVK RIDAGGRTGE
     PGSYTYDSAK VEKYTYYADG SLYTKEDRNG KMTAYEYDCH GRMLSQSVNG EAITYTYDRN
     GNQLEITDSA GKTTRTYDEQ GRVRTKAVPN IGTIEFRYDI IADMDPGCWA ETSIDPKGNT
     ITKIYDSEGR LWKVASEGKE TIYSYYGNGS KKGVEYSSGA REEYTYYKDG MLAALKNYVM
     QNGSEKLIDS YAYEYDAARN QISKDEYING SAKGTTVYEY DSLNRLKSVT EPGSSRTTVY
     TYDAAGNRQT EKVTENDGTV STQYNYNPQN RLDSTVTGYG GGIEETVRYS YDNNGNMTYK
     GVETTKPYDE TGEEKIEVYA GEEDKTDTDI AFYMYDDWNQ LVEISAGGQT SKYLYNGEGL
     RVGKEIGGKT TRYLYEYDNI ILEVDGEGNQ TGRNVYGTNL LMREVEGETL FYLYNGHGDV
     TSLVDTAGRA KVSYYYDAFG NILEQSGSAS NSITYAGYQY DDETGLYYLR SRMYDPVTAR
     FMQEDTYMGQ ASDPLSLNLY TYCHNEPIMY VDPTGHKEEL DKMIKSSATK TAIDKATKAY
     EQAKAKNDKA GMAKAHDDAQ KARSEYAKTS KDAHYIEAKY GTSALASYLG SGSSGKSSTQ
     GTGKDSSPAP NKGNDALKQQ IKTGMDKQLN NIASTQGTGK SGTSQGTGKS GTSQGTGNPK
     LGFDSLSNYK TRDQWGANPV NEKVGVERIK NPNQYFDSVV IHHTERATDE EIKHLQKYFQ
     DDRKYPDIGY HYIIGGGGTI YEGMPINLKG WHVEKNNTGK IGVVLTGNFN DGSGISGNVK
     DAINWLKGEG HTEPSKEQIE SLKQLIKVLD SQYGIDKVGG HKDFALSTSP SECPGNIAYP
     ILEKEGIIKL GK
//
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