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Database: UniProt
Entry: J6HEC4_9FIRM
LinkDB: J6HEC4_9FIRM
Original site: J6HEC4_9FIRM 
ID   J6HEC4_9FIRM            Unreviewed;      3157 AA.
AC   J6HEC4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Cna protein B-type domain protein {ECO:0000313|EMBL:EJU21103.1};
GN   ORFNames=HMPREF1143_1860 {ECO:0000313|EMBL:EJU21103.1};
OS   Peptoanaerobacter stomatis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoanaerobacter.
OX   NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU21103.1, ECO:0000313|Proteomes:UP000005244};
RN   [1] {ECO:0000313|EMBL:EJU21103.1, ECO:0000313|Proteomes:UP000005244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OBRC8 {ECO:0000313|EMBL:EJU21103.1,
RC   ECO:0000313|Proteomes:UP000005244};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000256|ARBA:ARBA00007257}.
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:EJU21103.1}.
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DR   EMBL; ALNK01000029; EJU21103.1; -; Genomic_DNA.
DR   RefSeq; WP_009531434.1; NZ_ALNK01000029.1.
DR   PATRIC; fig|796941.3.peg.1731; -.
DR   Proteomes; UP000005244; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR   Gene3D; 2.60.40.740; -; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   InterPro; IPR008456; Collagen-bd_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR041033; Prealbumin-like.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR36108:SF13; COLOSSIN-B; 1.
DR   PANTHER; PTHR36108; COLOSSIN-B-RELATED; 1.
DR   Pfam; PF05737; Collagen_bind; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF17802; SpaA; 6.
DR   SUPFAM; SSF49401; Bacterial adhesins; 2.
DR   SUPFAM; SSF49478; Cna protein B-type domain; 3.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005244};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3132..3150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3125..3157
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          2879..2953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2990..3043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2880..2894
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2922..2953
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3003..3042
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3157 AA;  353916 MW;  D15D68C8DBE326D2 CRC64;
     MYKFIKKYKK IFSILLAIGI FINMQYPYIN VLAEDINSLN TVSTTTGNQM LFGGAGTVRG
     GITFSNFEAN IVLQKVLSNA GEDNETTLDL TDKKVFDDAH ITLDTPLNLK IDTKIKETIR
     KDDIIDITLP DYPVDLSTFE DNEYTDSGFT YKIQIGSDGK KHIILKCLED IVLTSQPAEY
     ILKLPTKIKV QDHTKTKIEV PFDNGNTILT VNIAPKGITS SIQKSGLQEA NSIRWFIDIN
     LFSETISNFN IIENIPNEVI FDNNTTIVAK KLNIDLHGNK EIADEIISGV SKSISGNVAT
     ITVNEQIDYP IRIEFITPVK EDVVANSTTS TRIKNLAQFS STTSQAEVDF KPADMLEKTH
     ELVNFNDDKI SWKLTLNSAK TVIEDNKIKI TEAMSSNKKE NNHINSDEYT IDIPIKITIK
     NIDKNISRDV VPTGNGNNFE YEFERNDDEK NDTFEITYDT PIKNKISNIQ TKSLIENVAT
     TTLSGKNHSA TDTAEIVKSM HIKKSVNGIS KTADGYKSTW KISVNFDKHN IAPVVYDSIG
     LALTDNIKVL KDTIKVYEVT PQKIEDENHP DYIYWDARYT DESLVGSDKY TVSEITDTTR
     DFNISFNEQS NKAYVIKYDT LLDAPNDVVN TATLDGKSAS AGLGGNTHNR IYKYIKTHSE
     KKDNDYITVY DDLDMGNKTM LFYIYVEPNR APMKNIVIDD TFVNKGLSIE KEDISFSDTS
     ITDADFTFEK KTDATEGFKL SINKEISNRL EIKMIAHFTK NDNISTEKTH FPNKITANWK
     DKYNETNTNS NQVEYIIPQK LVDESYKNNS NISGTLHGGD IKDRLIDWTT NINYAGENLP
     ANTSVKIYPI KQDSSDDTTI IDERYHKIID DFKIYPYKLN KYGEIKYDMD HKLIENTDYT
     KTDNGDGSYT ITFLNPITTG YSIRYSTQID TKYTDDEKTN TEFDIYNKTK FKLKNEISVP
     PSTSVNITAI VDTKIREVFN KTGVQNKLNA YEINYTAIFN QIAEKVPQGT YIYDVLSEDQ
     IFMPDSLIMT YSNGTRVPEL DYVVNYSVDS KARHVMSIRF TKDIMEPIKI SYNAHVNNEN
     AKVLKNAISY KEDPTEVDVK DGSKITFKRK GSGRRIVPKG GSLINISYTN ESCCKNGKCP
     IFPNELEFEV IIKDSPTSTE TLYKTVKVGI NTKVPVNISA DKFVKVILKQ GPTANPKLRE
     FATEFKKTEE DKTTDVKYDV SLNEYKLKIK FEGDIGSRFD DTLAPDISLQ YSKNNASYNE
     KIDAITLKNA IKNLVSPNEY VVNVDTITQD MFKNSTNDKV KLQIPAGDVN LKNYKIELLS
     INGEPTADKN INNNEIVLDK CTENKIVVKI SRLKKHSITL KQWQSTAGVA GSFADNTVAN
     NKDIILKGTK VELKKNTVSN DYVLFEDIAE DIYDIIAPSI SYYITPEIST DFISTENSSA
     PNKVDVSESS FMTEHIATNT DALYKKAKKL IINKKEVIRK YDGSDETKTF NKDVTFTLTD
     KNDSNITAKF TVNSFTQKYK VVEDNSNIID VQGDVLYVKE GQYTLTEENM HSNYYYGYID
     LSDTKNLTSS SANNTSIDVD LSASVVNTDI SKEIYNHRDY NTLKITKTGD GIHPVTGTKI
     ALYTDVNGTE GTQIDEKTVD SSGTVTFENI SDLQYGYKET KAPDGYILDS KFYLIKRDSD
     TSGLILGRTE TKSLVNNRMK SKIVISKKDV SRDKYLIGVS FILQGTNENS QDVSAVKIQK
     NTEKIGDIAQ ASWDNLEVGT YKLYEKIPEG YTIPESYVNS DIVDNHIFTG YRIQINDNKK
     IYTVDDNNKN KGKIITDGKN ATVISNTALT LNFDVKKKSA NDDIAEKNNL PLKGVQYTLT
     EKTNSNIVGK FSKTVSTNEN GIAKFENIPV GEYELKEETT IDPYKKDTAV TTVKVENDNG
     NAKLIVGIDE NTNKLIEKTN SVDYGTLKIV KTAGNQRVNN VKFSIKYIAD INKIPAGFVN
     DITAPTNLQS HPYFKDRLYE ATTATVDSEN GVIKQKLPKG IYKITEVEAP DGYQKSAPYY
     VKVSGNDAIT TQTINNEVET VKLSIVKKDA NDNRLIKGAK FKIERKNNIN GSYEKLKNTD
     NTTIFTTNVS GKIEVTVQKG DIKITEITPA PHYSQNSLQL YDTVVEDSKK ISGELKITAD
     KTVIATNTKI KSKFVLNKKS VTRDNNSANF ANVEFKLYET DENYTKLDNI ADYTFTTDID
     GKIEEEINTG YYVIQETRKM GYTANIVVND NGTPILSNNF SFKKDINADT NISVENKPIY
     VKFKITKVKD GTNDAVQGAT VAIFDKNDTK IAEATSGADG VMNFDATYQN GVKQYDGILW
     QEGLYYKELN RPNGYFLNDN KHNITLNDDV SLNDSTINYT LGNKQILGEI KVITYSRNKL
     TNAEAKLGNI KVELEKYDGT SWQKIREATT DNNGEFVFTT LEEGKYRVVE KYASNTEVLK
     GYEQVDKEAT TTKGGTIKEV EIKPASADGK DTNGVTNHTL YISHEAFFGS LTINKKDTDG
     NKLTGVEFGL YDDSDKKIDT LITNDGTVKK ENLIFGNYYI KEEKTPNNIL MNTSKIDFSI
     NYGNRDVVKD ITNNKFEAKI EVSVIDSETN EPVDDTEISI INIGEKITDS TGKIIYTNVP
     KGKHNISISK VNPNYLPNHT VKKVELKDAD NNTIIKIEYK LTKIRTGIIL TKTDEKTGEK
     LQGIEFELKG TKVGNTTAIV KTTDEKGKII FDNLIYDTYT IKETQTKEEY RLLEDAITVE
     LNQENLVLDV KNTKKTGLLE FVTVDKNNKK PLRNAHIEIY KENKKIATFV TNEDGRAENI
     DTKDKNIYIV KDQVTNKNQI VMPIGKYTIK EIKAPNGYEL NKESMEFEIS LDTVMPVTLE
     NEPRPSSSDD EINGGNSGGF GGGGAGGNGG GIGDGGGGSS QTIPGIIFSL SNTSNNTTQM
     KTPESVTKSN TPENLTLNTF TNIVPIQNDI SNENLAQKKE DNLRQIYNAS KIPNGQMPVN
     IKPDKPATNT DNNIHEQSNN TAPNGNESAT KPNSTTTDNT KYKSNVEKIK KAIESKNVYE
     IVDKQNRHIG NARVVLKDDG VFLEFVNDSD VPLSGKIKYD EDDNSIELIE ENIPLSQINF
     ENKTLPKTGS NSNTATTISG FVLILLAILL KRKNKNI
//
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